ArticleProceedings of the National Academy of Sciences of the United States of America2002
Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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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, 79 citations in OpenAlex.
- Concussion-Related Biomarker Variations in Retired Rugby Players and Implications for Neurodegenerative Disease Risk: The UK Rugby Health Study.International journal of molecular sciences · 2024Article
- Acute-serum amyloid A and A-SAA-derived peptides as formyl peptide receptor (FPR) 2 ligands.Frontiers in endocrinology · 2023Review
- N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study.PloS one · 2022Article
- Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Soluble pattern recognition molecules: Guardians and regulators of homeostasis at airway mucosal surfaces.European journal of immunology · 2020Review
- Article
- Article
- Interleukin-1β Induces Intracellular Serum Amyloid A1 Expression in Human Coronary Artery Endothelial Cells and Promotes its Intercellular Exchange.Inflammation · 2019Article
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- Influence of C-terminal truncation of murine Serum amyloid A on fibril structure.Scientific reports · 2017Article
- Do's and don'ts of cryo-electron microscopy: a primer on sample preparation and high quality data collection for macromolecular 3D reconstruction.Journal of visualized experiments : JoVE · 2015Article
- Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A.Biochimie · 2014Article
- Endothelial injury markers before and after nasal continuous positive airway pressure treatment for obstructive sleep apnoea hypopnoea syndrome.Sleep & breathing = Schlaf & Atmung · 2014Article
- Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection.eLife · 2014Article
- Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The relationship between inflammatory biomarkers and telomere length in an occupational prospective cohort study.PloS one · 2014Article
- Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2.The Journal of biological chemistry · 2013Article
- Article
- Influence of the carboxy terminus of serum amyloid A on protein oligomerization, misfolding, and fibril formation.Biochemistry · 2012Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Serum amyloid A (SAA) is a small apolipoprotein that binds to high-density lipoproteins in the serum. Although SAA seems to play a role in host defense and lipid transport and metabolism, its specific functions have not been defined. Despite the growing implications that SAA plays a role in the pathology of various diseases, a high-resolution structure of SAA is lacking because of limited solubility in the high-density lipoprotein-free form. In this study, complementary methods including glutaraldehyde cross-linking, size-exclusion chromatography, and sedimentation-velocity analytical ultracentrifugation were used to show that murine SAA2.2 in aqueous solution exists in a monomer-hexamer equilibrium. Electron microscopy of hexameric SAA2.2 revealed that the subunits are arranged in a ring forming a putative central channel. Limited trypsin proteolysis and mass spectrometry analysis identified a significantly protease-resistant SAA2.2 region comprising residues 39-86. The isolated 39-86 SAA2.2 fragment did not hexamerize, suggesting that part of the N terminus is involved in SAA2.2 hexamer formation. Circular-dichroism spectrum deconvolution and secondary-structure prediction suggest that SAA2.2 contains approximately 50% of its residues in alpha-helical conformation and <10% in beta-structure. These findings are consistent with the recent discovery that human SAA1.1 forms a membrane channel and have important implications for understanding the 3D structure, multiple functions, and pathological roles of this highly conserved protein.
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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.