Virender Pratap Singh

Reply to: Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy

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

Polymorphic IGLV6-57 AL amyloid fibrils and features of a shared folding pathway

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

Structural polymorphism of ex-vivo ALECT2 amyloid fibrils revealed by cryo-EM

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

A Shared Amyloid Architecture in Cardiac Fibrils from Three Neuropathy-Associated ATTR Variants

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.

Structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations, revealed by cryo-EM

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.

ATTRv-V30M Type A amyloid fibrils from the heart and nerves exhibit structural homogeneity.

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.

Multi-organ structural homogeneity of amyloid fibrils in ATTRv-T60A amyloidosis patients, revealed by Cryo-EM

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

Amyloid fibril polymorphism in the heart and the liver of an ATTR amyloidosis patient with polyneuropathy attributed to the ATTRv-V122Δ variant

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.

Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis

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

Structural polymorphism of amyloid fibrils in cardiac ATTR amyloidosis revealed by cryo-electron microscopy

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.