ArticleNature communications2022
Amyloid fibril structure from the vascular variant of systemic AA amyloidosis.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Destabilization of Helix III Initiates Early Serum Amyloid A Misfolding by Exposing Its Amyloidogenic Core.The journal of physical chemistry letters · 2025Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- 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
- Polymorphisms in SAA alter intrarenal amyloid distribution of AA amyloidosis in cats.Scientific reports · 2025Article
- Epidemiology and clinical presentation of kidney amyloidosis have changed over the past three decades: a nationwide population-based study.BMC nephrology · 2025Article
- Serum Amyloid A Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis.Journal of molecular biology · 2025Article
- The question of strains in AA amyloidosis.Scientific reports · 2025Article
- ATTRv-V30M amyloid fibrils from heart and nerves exhibit structural homogeneity.Structure (London, England : 1993) · 2024Article
- Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis.Nature communications · 2024Article
- ATTRv-V30M Type A amyloid fibrils from heart and nerves exhibit structural homogeneity.bioRxiv : the preprint server for biology · 2024Article
- Structural polymorphism of amyloid fibrils in ATTR amyloidosis revealed by cryo-electron microscopy.Nature communications · 2024Article
- Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils.Nature communications · 2024Article
- Common transthyretin-derived amyloid fibril structures in patients with hereditary ATTR amyloidosis.Nature communications · 2023Article
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Authors and funding
15 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Systemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called 'vascular' and 'glomerular', depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies.
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