Rose Pedretti

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.

The paper determines the cryo-EM structures of three neuropathy-associated ATTR variants and reveals a shared amyloid core despite different mutations and clinical phenotypes.

The paper detects ATTR aggregates in plasma of polyneuropathic ATTR-V30M amyloidosis patients using a peptide probe and finds no correlation with age or gender.

The paper uses cryo-EM to show that cardiac ATTRwt amyloid fibrils from four patients are structurally identical, supporting their consistent clinical presentation.

The paper develops a peptide probe based on cryogenic electron microscopy structures to detect large transthyretin aggregates in ATTR amyloidosis patients' plasma, revealing previously unknown aggregated species.

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.

The paper uses cryo-electron microscopy to show that cardiac ATTR amyloid fibrils are structurally polymorphic, independent of genotype and phenotype, challenging the one-fibril-fold-per-disease paradigm.