María del Carmen Fernández‐Ramírez

This study identifies an N-terminal ATTR fibril segment that promotes TTR amyloid nucleation and polymorphism through structural compatibility and templating activity.

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.

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.

This study determines the structure of ATTRv-V30M amyloid fibrils from cardiac and nerve tissues using cryo-EM, finding structural homogeneity across tissues when transthyretin originates from the liver.

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.

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.

The paper compares the amyloid-like assembly mechanisms of CPEB prion-like domains from Aplysia and Drosophila, showing divergent pathways leading to a common fold.