ArticleScientific reports2017
Influence of C-terminal truncation of murine Serum amyloid A on fibril structure.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 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
- Serum Amyloid A: A Double-Edged Sword in Health and Disease.International journal of molecular sciences · 2025Review
- Viruses and amyloids - a vicious liaison.Prion · 2023Review
- Cryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril.Journal of molecular biology · 2023Article
- Revisiting misfolding propensity of serum amyloid A1: Special focus on the signal peptide region.Biochemistry and biophysics reports · 2022Article
- Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding.Nature communications · 2022Article
- SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study.Journal of structural biology: X · 2022Article
- AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils.Nature communications · 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
- Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer's brain tissue.Nature communications · 2019Article
- Article
- Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids.Nature communications · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloid A (AA) amyloidosis is a systemic protein misfolding disease affecting humans and other vertebrates. While the protein precursor in humans and mice is the acute-phase reactant serum amyloid A (SAA) 1.1, the deposited fibrils consist mainly of C-terminally truncated SAA fragments, termed AA proteins. For yet unknown reasons, phenotypic variations in the AA amyloid distribution pattern are clearly associated with specific AA proteins. Here we describe a bacterial expression system and chromatographic strategies to obtain significant amounts of C-terminally truncated fragments of murine SAA1.1 that correspond in truncation position to relevant pathological AA proteins found in humans. This enables us to investigate systematically structural features of derived fibrils. All fragments form fibrils under nearly physiological conditions that show similar morphological appearance and amyloid-like properties as evident from amyloid-specific dye binding, transmission electron microscopy and infrared spectroscopy. However, infrared spectroscopy suggests variations in the structural organization of the amyloid fibrils that might be derived from a modulating role of the C-terminus for the fibril structure. These results provide insights, which can help to get a better understanding of the molecular mechanisms underlying the different clinical phenotypes of AA amyloidosis.
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