ArticleThe journal of physical chemistry. B2022
Effect of an Amyloidogenic SARS-COV-2 Protein Fragment on α-Synuclein Monomers and Fibrils.
Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Stability and Dynamics of the N‑Terminal Domain of TDP-43 and the Effect of Point Mutations.ACS omega · 2026Article
- The Effect of SARS-COV-2 Protein Fragments on the Dimerization of α-Synuclein.ACS chemical neuroscience · 2025Article
- Modulation of AβJournal of chemical information and modeling · 2025Article
- An Amyloidogenic Fragment of the Spike Protein from SARS-CoV-2 Virus Stimulates the Aggregation and Toxicity of Parkinson's Disease Protein Alpha-Synuclein.ACS chemical neuroscience · 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
- Coupling of SARS-CoV-2 to Aβ Amyloid Fibrils.ACS omega · 2024Article
- Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.The Journal of chemical physics · 2024Article
- Alpha-synuclein dynamics bridge Type-I Interferon response and SARS-CoV-2 replication in peripheral cells.Biological research · 2024Article
- Infections in the Etiology of Parkinson's Disease and Synucleinopathies: A Renewed Perspective, Mechanistic Insights, and Therapeutic Implications.Journal of Parkinson's disease · 2024Review
- Spike Protein Fragments Promote Alzheimer's Amyloidogenesis.ACS applied materials & interfaces · 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
- Aggregation-Seeding Forms of α-Synuclein Are Not Detected in Acute Coronavirus Disease 2019 Cerebrospinal Fluid.Movement disorders : official journal of the Movement Disorder Society · 2022Article
- Investigating neurological symptoms of infectious diseases like COVID-19 leading to a deeper understanding of neurodegenerative disorders such as Parkinson's disease.Frontiers in neurology · 2022Review
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4 authors.
Funding
Abstract
Aggregates of α-synuclein are thought to be the disease-causing agent in Parkinson's disease. Various case studies have hinted at a correlation between COVID-19 and the onset of Parkinson's disease. For this reason, we use molecular dynamics simulations to study whether amyloidogenic regions in SARS-COV-2 proteins can initiate and modulate aggregation of α-synuclein. As an example, we choose the nine-residue fragment SFYVYSRVK (SK9), located on the C-terminal of the envelope protein of SARS-COV-2. We probe how the presence of SK9 affects the conformational ensemble of α-synuclein monomers and the stability of two resolved fibril polymorphs. We find that the viral protein fragment SK9 may alter α-synuclein amyloid formation by shifting the ensemble toward aggregation-prone and preferentially rod-like fibril seeding conformations. However, SK9 has only a small effect on the stability of pre-existing or newly formed fibrils. A potential mechanism and key residues for potential virus-induced amyloid formation are described.
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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.