Preeti Singh

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

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

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 cardiac ATTRwt amyloid fibrils from four patients are structurally identical, supporting their consistent clinical presentation.

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.