ArticleEMBO reports2017
Cellular mechanism of fibril formation from serum amyloid A1 protein.
Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Assessment of the biochemical basis underlying the resistance against systemic amyloidosis.Scientific reports · 2026Article
- Homeostatic microglia initially seed and activated microglia later reshape amyloid plaques in Alzheimer's Disease.Nature communications · 2024Article
- The ASC inflammasome adapter governs SAA-derived protein aggregation in inflammatory amyloidosis.EMBO molecular medicine · 2024Article
- Review
- Deficiency of circadian clock gene Bmal1 exacerbates noncanonical inflammasome-mediated pyroptosis and lethality via Rev-erbα-C/EBPβ-SAA1 axis.Experimental & molecular medicine · 2024Article
- Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter.Nature communications · 2022Article
- SARS-CoV-2-Induced Amyloidgenesis: Not One, but Three Hypotheses for Cerebral COVID-19 Outcomes.Metabolites · 2022Article
- Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding.Nature communications · 2022Article
- Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.Biophysical chemistry · 2022Review
- AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.Nature communications · 2021Article
- Serum Amyloid A1 Induces Classically Activated Macrophages: A Role for Enhanced Fibril Formation.Frontiers in immunology · 2021Article
- Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve.Current atherosclerosis reports · 2020Review
- Irradiation effect of a submillimeter wave from 420 GHz gyrotron on amyloid peptides in vitro.Biomedical optics express · 2020Article
- Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A.Journal of molecular biology · 2020Article
- Article
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- High-density lipoprotein inhibits serum amyloid A-mediated reactive oxygen species generation and NLRP3 inflammasome activation.The Journal of biological chemistry · 2018Article
- Effect of Phosphatidylserine and Cholesterol on Membrane-mediated Fibril Formation by the N-terminal Amyloidogenic Fragment of Apolipoprotein A-I.Scientific reports · 2018Article
- Serum amyloid A sequesters diverse phospholipids and their hydrolytic products, hampering fibril formation and proteolysis in a lipid-dependent manner.Chemical communications (Cambridge, England) · 2018Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serum amyloid A1 (SAA1) is an apolipoprotein that binds to the high-density lipoprotein (HDL) fraction of the serum and constitutes the fibril precursor protein in systemic AA amyloidosis. We here show that HDL binding blocks fibril formation from soluble SAA1 protein, whereas internalization into mononuclear phagocytes leads to the formation of amyloid. SAA1 aggregation in the cell model disturbs the integrity of vesicular membranes and leads to lysosomal leakage and apoptotic death. The formed amyloid becomes deposited outside the cell where it can seed the fibrillation of extracellular SAA1. Our data imply that cells are transiently required in the amyloidogenic cascade and promote the initial nucleation of the deposits. This mechanism reconciles previous evidence for the extracellular location of deposits and amyloid precursor protein with observations the cells are crucial for the formation of amyloid.
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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.