ArticleCommunications biology2024
Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis.
Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The causative role of amyloidosis in the cardiac complications of Alzheimer's disease: a comprehensive systematic review.The Journal of physiology · 2026Pooled it
- Structural Hierarchy and Maturation of Amyloid Fibrils Revealed by Interface Descriptor Analysis.Journal of chemical information and modeling · 2026Article
- 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
- Transthyretin amyloid fibrils adopt distinct folds in the brain.bioRxiv : the preprint server for biology · 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
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.Nature communications · 2025Article
- Structural characterization of atrial natriuretic peptide amyloid fibrils from patients with atrial fibrillation.Nature communications · 2025Article
- A Shared Amyloid Architecture in Cardiac Fibrils from Three Neuropathy-Associated ATTR Variants.bioRxiv : the preprint server for biology · 2025Article
- ATTRv-V30M amyloid fibrils from heart and nerves exhibit structural homogeneity.Structure (London, England : 1993) · 2024Article
- ATTRv-V30M Type A amyloid fibrils from heart and nerves exhibit structural homogeneity.bioRxiv : the preprint server for biology · 2024Article
- Multi-organ structural homogeneity of amyloid fibrils in ATTRv-T60A amyloidosis patients, revealed by Cryo-EM.bioRxiv : the preprint server for biology · 2024Article
- Amyloid fibril polymorphism in the heart of an ATTR amyloidosis patient with polyneuropathy attributed to the V122Δ variant.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
- Update of
Authors and funding
13 authors.
Funding
Abstract
ATTR amyloidosis results from the conversion of transthyretin into amyloid fibrils that deposit in tissues causing organ failure and death. This conversion is facilitated by mutations in ATTRv amyloidosis, or aging in ATTRwt amyloidosis. ATTRv amyloidosis exhibits extreme phenotypic variability, whereas ATTRwt amyloidosis presentation is consistent and predictable. Previously, we found unique structural variabilities in cardiac amyloid fibrils from polyneuropathic ATTRv-I84S patients. In contrast, cardiac fibrils from five genotypically different patients with cardiomyopathy or mixed phenotypes are structurally homogeneous. To understand fibril structure's impact on phenotype, it is necessary to study the fibrils from multiple patients sharing genotype and phenotype. Here we show the cryo-electron microscopy structures of fibrils extracted from four cardiomyopathic ATTRwt amyloidosis patients. Our study confirms that they share identical conformations with minimal structural variability, consistent with their homogenous clinical presentation. Our study contributes to the understanding of ATTR amyloidosis biopathology and calls for further studies.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.