ArticleInternational journal of molecular sciences2021
S100A9 Alters the Pathway of Alpha-Synuclein Amyloid Aggregation.
Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Nickel(II) and Zinc(II) Binding to Tau Protein Fragments Containing Histidine and Cysteine.Biological trace element research · 2026Article
- Heterotypic Droplet Formation by Pro-Inflammatory S100A9 and Neurodegenerative Disease-Related α-Synuclein.Biomacromolecules · 2025Article
- Imidazo[2,1-ACS chemical neuroscience · 2024Article
- Human Leukocyte Antigen Polymorphism and Blood Biomarker Profiles in Parkinson's Disease: A Pilot Study in a Latvian Cohort.Biomedicines · 2024Article
- Structural basis of epitope recognition by anti-alpha-synuclein antibodies MJFR14-6-4-2.NPJ Parkinson's disease · 2024Article
- Morphological and Biophysical Study of S100A9 Protein Fibrils by Atomic Force Microscopy Imaging and Nanomechanical Analysis.Biomolecules · 2024Article
- Synucleinopathies: Intrinsic and Extrinsic Factors.Cell biochemistry and biophysics · 2023Article
- Conformation-Specific Association of Prion Protein Amyloid Aggregates with Tau Protein Monomers.International journal of molecular sciences · 2023Article
- Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid.Biomedicines · 2023Article
- Targeting neuronal lysosomal dysfunction caused by β-glucocerebrosidase deficiency with an enzyme-based brain shuttle construct.Nature communications · 2023Article
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- Interactions between S100A9 and Alpha-Synuclein: Insight from NMR Spectroscopy.International journal of molecular sciences · 2022Article
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- Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
The formation of amyloid fibril plaques in the brain creates inflammation and neuron death. This process is observed in neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases. Alpha-synuclein is the main protein found in neuronal inclusions of patients who have suffered from Parkinson's disease. S100A9 is a calcium-binding, pro-inflammation protein, which is also found in such amyloid plaques. To understand the influence of S100A9 on the aggregation of α-synuclein, we analyzed their co-aggregation kinetics and the resulting amyloid fibril structure by Fourier-transform infrared spectroscopy and atomic force microscopy. We found that the presence of S100A9 alters the aggregation kinetics of α-synuclein and stabilizes the formation of a particular amyloid fibril structure. We also show that the solution's ionic strength influences the interplay between S100A9 and α-synuclein, stabilizing a different structure of α-synuclein fibrils.
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