ArticleNature communications2019
Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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110 citing papers in PubMed.
- An N-terminal ATTR Fibril Segment Promotes Transthyretin Amyloid Nucleation and Polymorphism.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures of biopsy-derived TTR fibrils in hereditary transthyretin amyloidosis.Nature communications · 2026Article
- Cryo-EM structures of ALECT2 filaments from human renal biopsies.Nature communications · 2026Article
- Transthyretin amyloid fibrils adopt distinct folds in the brain.bioRxiv : the preprint server for biology · 2026Article
- Induced Circular Dichroism From the Binding of Achiral Bivalent Ligands to Transthyretin.Journal of molecular recognition : JMR · 2026Article
- Structures of dye-bound transthyretin amyloid fibrils from abdominal fat biopsies.Nature communications · 2026Article
- Amyloid fibril polymorphism in the heart and liver of a patient with polyneuropathic ATTRv-V122Δ amyloidosis.Communications biology · 2026Article
- 3D Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary Occlusion.bioRxiv : the preprint server for biology · 2026Article
- Glycosidic scaffold bearing multiple galloyl moieties from pomegranate disrupts transthyretin amyloids.iScience · 2026Article
- CRISPR-Cas3-based editing for targeted deletions in a mouse model of transthyretin amyloidosis.Nature biotechnology · 2026Article
- Context-tuned strategies for marker selection precision in neuronal studies.Frontiers in neuroscience · 2026Review
- Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.Nature communications · 2025Article
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation.Nature communications · 2025Article
- Structural characterization of atrial natriuretic peptide amyloid fibrils from patients with atrial fibrillation.Nature communications · 2025Article
- In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential.Cardiovascular research · 2025Review
- Apolipoprotein A-IV fibrils: structural diagnosis of mixed cardiac amyloidosis.Nature communications · 2025Article
- Pan-Amyloid Reactive Peptides p5+14 and p5R Exhibit Specific Charge-Dependent Binding to Glycosaminoglycans.Pharmaceuticals (Basel, Switzerland) · 2025Article
- A Shared Amyloid Architecture in Cardiac Fibrils from Three Neuropathy-Associated ATTR Variants.bioRxiv : the preprint server for biology · 2025Article
- Cryo-EM of wild-type and mutant PMEL amyloid cores reveals structural mechanism of pigment dispersion syndrome.Nature communications · 2025Article
50 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ATTR amyloidosis is one of the worldwide most abundant forms of systemic amyloidosis. The disease is caused by the misfolding of transthyretin protein and the formation of amyloid deposits at different sites within the body. Here, we present a 2.97 Å cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30Met ATTR amyloidosis. The fibril consists of a single protofilament that is formed from an N-terminal and a C-terminal fragment of transthyretin. Our structure provides insights into the mechanism of misfolding and implies the formation of an early fibril state from unfolded transthyretin molecules, which upon proteolysis converts into mature ATTR amyloid fibrils.
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