ReviewCurrent atherosclerosis reports2020
Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve.
Review in Current atherosclerosis reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Surface cues shape procoagulant properties of amyloidogenic microclots.Cell death & disease · 2026Review
- Assessment of the biochemical basis underlying the resistance against systemic amyloidosis.Scientific reports · 2026Article
- MarkerPredict: predicting clinically relevant predictive biomarkers with machine learning.NPJ systems biology and applications · 2025Article
- Elevated Serum Amyloid A2 and A4 in Patients With Guillain-Barré Syndrome.Journal of clinical neurology (Seoul, Korea) · 2025Article
- Serum Amyloid A Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis.Journal of molecular biology · 2025Article
- Functional Interactions Between Recombinant Serum Amyloid A1 (SAA1) and Chemokines in Leukocyte Recruitment.International journal of molecular sciences · 2025Review
- Recent Advances in Studies of Serum Amyloid A: Implications in Inflammation, Immunity and Tumor Metastasis.International journal of molecular sciences · 2025Review
- Balancing inflammation: the specific roles of serum amyloid A proteins in sterile and infectious diseases.Frontiers in immunology · 2025Article
- Article
- Asthmatic patients with high serum amyloid A have proinflammatory HDL: Implications for augmented systemic and airway inflammation.The Journal of allergy and clinical immunology · 2024Article
- AA amyloidosis With Ig-Dominant Staining and Diagnostically Unusual Features.Kidney international reports · 2024Article
- Research progress of biomarkers in evaluating the severity and prognostic value of severe pneumonia in children.Frontiers in pediatrics · 2024Review
- Selenoprotein S: A versatile disordered protein.Archives of biochemistry and biophysics · 2022Review
- Amyloid fibril structure from the vascular variant of systemic AA amyloidosis.Nature communications · 2022Article
- Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.Biophysical chemistry · 2022Review
- Adaptation of Microarray Assay for Serum Amyloid a Analysis in Human Serum.Molecular biology · 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
- Article
- The Etiology and Pathophysiology Genesis of Benign Prostatic Hyperplasia and Prostate Cancer: A New Perspective.Medicines (Basel, Switzerland) · 2021Review
- Connection between the Altered HDL Antioxidant and Anti-Inflammatory Properties and the Risk to Develop Alzheimer's Disease: A Narrative Review.Oxidative medicine and cellular longevity · 2021Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
purpose of reviewThis review addresses normal and pathologic functions of serum amyloid A (SAA), an enigmatic biomarker of inflammation and protein precursor of AA amyloidosis, a life-threatening complication of chronic inflammation. SAA is a small, highly evolutionarily conserved acute-phase protein whose plasma levels increase up to one thousand-fold in inflammation, infection, or after trauma. The advantage of this dramatic but transient increase is unclear, and the complex role of SAA in immune response is intensely investigated. This review summarizes recent advances in our understanding of the structure-function relationship of this intrinsically disordered protein, outlines its newly emerging beneficial roles in lipid transport and inflammation control, and discusses factors that critically influence its misfolding in AA amyloidosis. RECENT
findingsHigh-resolution structures of lipid-free SAA in crystals and fibrils have been determined by x-ray crystallography and electron cryo-microscopy. Low-resolution structural studies of SAA-lipid complexes, together with biochemical, cell-based, animal model, genetic, and clinical studies, have provided surprising new insights into a wide range of SAA functions. An emerging vital role of SAA is lipid encapsulation to remove cell membrane debris from sites of injury. The structural basis for this role has been proposed. The lysosomal origin of AA amyloidosis has solidified, and its molecular and cellular mechanisms have emerged. Recent studies have revealed molecular underpinnings for understanding complex functions of this Cambrian protein in lipid transport, immune response, and amyloid formation. These findings help guide the search for much-needed targeted therapies to block the protein deposition in AA amyloidosis.
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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.