Binh An Nguyen

The paper identifies sequence changes that bias tau aggregation toward CTE-like structures using mutagenesis and structural analysis.

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

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 identifies cysteine residues as critical for tau aggregation and propagation in cells, both spontaneously and when seeded.

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 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-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.