ArticleThe journal of physical chemistry. B2021
Presence of a SARS-CoV-2 Protein Enhances Amyloid Formation of Serum Amyloid A.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
29 citing papers in PubMed, 45 citations in OpenAlex.
- Primary (AL) Amyloidosis Following COVID-19 Infection: A Case Report.Clinical case reports · 2026Article
- Modulation of AβJournal of chemical information and modeling · 2025Article
- Coupling of SARS-CoV-2 to Amyloid Fibrils and Liquid-Liquid Phase Separation.Current protein & peptide science · 2025Review
- Effect of a SARS-CoV-2 Protein Fragment on the Amyloidogenic Propensity of Human Islet Amyloid Polypeptide.ACS chemical neuroscience · 2024Article
- Article
- Coronavirus Disease 2019 Outcomes in Amyloid A Protein Amyloidosis Secondary to Rheumatic Conditions and Signs of Post- Coronavirus Disease 2019 Proteinuria Progression.European journal of rheumatology · 2024Article
- Coupling of SARS-CoV-2 to Aβ Amyloid Fibrils.ACS omega · 2024Article
- Neurological sequelae of long COVID: a comprehensive review of diagnostic imaging, underlying mechanisms, and potential therapeutics.Frontiers in neurology · 2024Review
- Exploring the Potential Long-term Impact of SARS-CoV-2 on Protein Misfolding and Amyloid-related Conditions.Protein and peptide letters · 2024Review
- Extracellular vesicles derived from SARS-CoV-2 M-protein-induced triple negative breast cancer cells promoted the ability of tissue stem cells supporting cancer progression.Frontiers in oncology · 2024Article
- Article
- Gastrointestinal AA Amyloidosis following Recurrent SARS-CoV-2 Infection: A Case Report.Yonsei medical journal · 2023Article
- SARS-COV-2 spike protein fragment eases amyloidogenesis of α-synuclein.The Journal of chemical physics · 2023Article
- SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein.bioRxiv : the preprint server for biology · 2023Article
- Human Amylin in the Presence of SARS-COV-2 Protein Fragments.ACS omega · 2023Article
- Pathogenesis Underlying Neurological Manifestations of Long COVID Syndrome and Potential Therapeutics.Cells · 2023Review
- Non-alcoholic fatty liver disease and liver secretome.Archives of pharmacal research · 2022Review
- Elevated Serum Amyloid A Levels Contribute to Increased Platelet Adhesion in COVID-19 Patients.International journal of molecular sciences · 2022Article
- SARS-CoV-2-Induced Amyloidgenesis: Not One, but Three Hypotheses for Cerebral COVID-19 Outcomes.Metabolites · 2022Article
- The deciphering of the immune cells and marker signature in COVID-19 pathogenesis: An update.Journal of medical virology · 2022Review
Corrections and comments
- Update of
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. To understand whether SAA amyloidosis could also be a long-term risk of SARS-CoV-2 infections, we have used long all-atom molecular dynamic simulations to study the effect of a SARS-CoV-2 protein segment on SAA amyloid formation. Sampling over 40 μs, we find that the presence of the nine-residue segment SK9, located at the C-terminus of the envelope protein, increases the propensity for SAA fibril formation by three mechanisms: it reduces the stability of the lipid-transporting hexamer shifting the equilibrium toward monomers, it increases the frequency of aggregation-prone configurations in the resulting chains, and it raises the stability of SAA fibrils. Our results therefore suggest that SAA amyloidosis and related pathologies may be a long-term risk of SARS-CoV-2 infections.
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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.