ArticleNature communications2021
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Bioinformatic assessment of the potential amyloidogenicity of the human and evolutionarily more ancient proteomes.The Biochemical journal · 2026Article
- Cryo-EM of Cardiac AL-224L Amyloid Reveals Shared Structural Motifs and Mutation-induced Differences in λ6 Light Chain Fibrils.Journal of molecular biology · 2026Article
- Assessment of the biochemical basis underlying the resistance against systemic amyloidosis.Scientific reports · 2026Article
- Inhibiting Disulfide Bonding in Truncated Tau297-391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies.ACS chemical neuroscience · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Identifying the quantity profiles of amyloid signature proteins in different types of renal amyloidosis.BMC nephrology · 2025Article
- Elucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A.Biochemistry · 2025Article
- Identification and characterization of spontaneous AA amyloidosis in CD-1 mice used in toxicity studies: implications of SAA1 and SAA2 copy number variations.Journal of toxicologic pathology · 2025Article
- Water-protein interactions as a driver of phase separation, biology, and disease.Biophysical journal · 2024Article
- Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis.Nature communications · 2024Article
- Real-Time 3D Imaging and Inhibition Analysis of Human Serum Amyloid A Aggregations Using Quantum Dots.International journal of molecular sciences · 2024Article
- Hierarchical Protofilament Intertwining Rules the Formation of Mixed-Curvature Amyloid Polymorphs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- AA Amyloidosis: A Contemporary View.Current rheumatology reports · 2024Review
- Structural insight intomBio · 2024Article
- Molecular Crowding: The History and Development of a Scientific Paradigm.Chemical reviews · 2024Review
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils.Nature communications · 2024Article
- Article
- Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril.Nature communications · 2023Article
- Simulations of Amyloid-Forming Peptides in the Crystal State.The protein journal · 2023Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher β-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue.
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