ArticleFEBS letters2016
Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 53 citations in OpenAlex.
- Surface cues shape procoagulant properties of amyloidogenic microclots.Cell death & disease · 2026Review
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- 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 Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis.Journal of molecular biology · 2025Article
- Molecular insights into the unique properties of the blood-circulating proteasome.Journal of extracellular biology · 2025Article
- Longitudinal Fluctuations in Protein Concentrations and Higher-Order Structures in the Plasma Proteome of Kidney Failure Patients Subjected to a Kidney Transplant.Journal of proteome research · 2024Article
- Can "Bad" HDL Be Turned Good Again?Arteriosclerosis, thrombosis, and vascular biology · 2023Article
- Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter.Nature communications · 2022Article
- Human Serum Amyloid a Impaired Structural Stability of High-Density Lipoproteins (HDL) and Apolipoprotein (Apo) A-I and Exacerbated Glycation Susceptibility of ApoA-I and HDL.Molecules (Basel, Switzerland) · 2022Article
- Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.Biophysical chemistry · 2022Review
- Review
- High-Density Lipoprotein (HDL) in Allergy and Skin Diseases: Focus on Immunomodulating Functions.Biomedicines · 2020Review
- 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
- Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A.Journal of molecular biology · 2020Article
- Expression and clinical significance of serum amyloid A and interleukin-6 in patients with acute exacerbation of chronic obstructive pulmonary disease.Experimental and therapeutic medicine · 2020Article
- Serum amyloid A exhibits pH dependent antibacterial action and contributes to host defense againstThe Journal of biological chemistry · 2020Article
- Serum Amyloid A1 (SAA1) Revisited: Restricted Leukocyte-Activating Properties of Homogeneous SAA1.Frontiers in immunology · 2020Article
- Article
- Intestinal Serum amyloid A suppresses systemic neutrophil activation and bactericidal activity in response to microbiota colonization.PLoS pathogens · 2019Article
- Expression of SAA1, SAA2 and SAA4 genes in human primary monocytes and monocyte-derived macrophages.PloS one · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Serum amyloid A is a major acute-phase plasma protein that modulates innate immunity and cholesterol homeostasis. We combine sequence analysis with x-ray crystal structures to postulate that SAA acts as an intrinsically disordered hub mediating interactions among proteins, lipids and proteoglycans. A structural model of lipoprotein-bound SAA monomer is proposed wherein two α-helices from the N-domain form a concave hydrophobic surface that binds lipoproteins. A C-domain, connected to the N-domain via a flexible linker, binds polar/charged ligands including cell receptors, bridging them with lipoproteins and rerouting cholesterol transport. Our model is supported by the SAA cleavage in the interdomain linker to generate the 1-76 fragment deposited in reactive amyloidosis. This model sheds new light on functions of this enigmatic protein.
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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.