ArticleChemistry (Weinheim an der Bergstrasse, Germany)2018
Alpha-Synuclein Modulates the Physical Properties of DNA.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- DNA Modulates Structural Transitions and Oligomerization Kinetics of the Functional Amyloid CRES.Journal of the American Chemical Society · 2026Article
- ATP Hydrolysis by α-Synuclein Amyloids is Mediated by Enclosing β-Strand.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Biological Amyloids Chemically Damage DNA.ACS chemical neuroscience · 2025Article
- Lipids and α-Synuclein: adding further variables to the equation.Frontiers in molecular biosciences · 2024Review
- Alpha-Synuclein Contribution to Neuronal and Glial Damage in Parkinson's Disease.International journal of molecular sciences · 2023Review
- Determining the Location of the α-Synuclein Dimer Interface Using Native Top-Down Fragmentation and Isotope Depletion-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Constitutive nuclear accumulation of endogenous alpha-synuclein in mice causes motor impairment and cortical dysfunction, independent of protein aggregation.Human molecular genetics · 2022Article
- α-synucleinopathy exerts sex-dimorphic effects on the multipurpose DNA repair/redox protein APE1 in mice and humans.Progress in neurobiology · 2022Article
- Pathogenic Impact of α-Synuclein Phosphorylation and Its Kinases in α-Synucleinopathies.International journal of molecular sciences · 2022Review
- Occurrence of Total and Proteinase K-Resistant Alpha-Synuclein in Glioblastoma Cells Depends on mTOR Activity.Cancers · 2022Article
- Modulation of the Conformational Space of SARS-CoV-2 RNA Quadruplex RG-1 by Cellular Components and the Amyloidogenic Peptides α-Synuclein and hIAPP.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- An Update on the Critical Role of α-Synuclein in Parkinson's Disease and Other Synucleinopathies: from Tissue to Cellular and Molecular Levels.Molecular neurobiology · 2022Review
- Brain regions susceptible to alpha-synuclein spreading.Molecular psychiatry · 2022Review
- Molecular insights into α-synuclein interaction with individual human core histones, linker histone, and dsDNA.Protein science : a publication of the Protein Society · 2021Article
- Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.RSC chemical biology · 2021Article
- Epigenetics of Aging and Aging-Associated Diseases.International journal of molecular sciences · 2021Review
- Imaging of α-Synuclein Aggregates in a Rat Model of Parkinson's Disease Using Raman Microspectroscopy.Frontiers in cell and developmental biology · 2021Article
- Alteration of the Conformational Dynamics of a DNA Hairpin by α-Synuclein in the Presence of Aqueous Two-Phase Systems.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Crosstalk Between Alpha-Synuclein and Other Human and Non-Human Amyloidogenic Proteins: Consequences for Amyloid Formation in Parkinson's Disease.Journal of Parkinson's disease · 2020Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Fundamental research on Parkinson's disease (PD) most often focuses on the ability of α-synuclein (aS) to form oligomers and amyloids, and how such species promote brain cell death. However, there are indications that aS also plays a gene-regulatory role in the cell nucleus. Here, the interaction between monomeric aS and DNA in vitro has been investigated with single-molecule techniques. Using a nanofluidic channel system, it was discovered that aS binds to DNA and by studying the DNA-protein complexes at different confinements we determined that aS binding increases the persistence length of DNA from 70 to 90 nm at high coverage. By atomic force microscopy it was revealed that at low protein-to-DNA ratio, the aS binding occurs as small protein clusters scattered along the DNA; at high protein-to-DNA ratio, the DNA is fully covered by protein. As DNA-aS interactions may play roles in PD, it is of importance to characterize biophysical properties of such complexes in detail.
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Registered trials
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