ArticleBiochemistry2013
α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Neuroimmune Interactions in Neurodegeneration: The Role of Microglia in Alzheimer's and Parkinson's Disease Pathogenesis.Brain sciences · 2026Review
- On Levodopa Interactions with Brain Disease Amyloidogenic Proteins at the Nanoscale.ACS omega · 2025Article
- 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
- Wild-TypeFrontiers in molecular biosciences · 2022Article
- Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get.Journal of neurochemistry · 2021Article
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.Nature communications · 2020Article
- AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020Article
- Spontaneous self-assembly of amyloid β (1-40) into dimers.Nanoscale advances · 2019Article
- Probing the Basis of α-Synuclein Aggregation by Comparing Simulations to Single-Molecule Experiments.Biophysical journal · 2019Article
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.Bioconjugate chemistry · 2018Article
- A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Protein science : a publication of the Protein Society · 2018Article
- High-speed atomic force microscopy reveals structural dynamics of α-synuclein monomers and dimers.The Journal of chemical physics · 2018Article
- Polymer Nanoarray Approach for the Characterization of Biomolecular Interactions.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Single-molecule probing of amyloid nano-ensembles using the polymer nanoarray approach.Physical chemistry chemical physics : PCCP · 2017Article
- Nano-assembly of amyloid β peptide: role of the hairpin fold.Scientific reports · 2017Article
- Effect of acidic pH on the stability of α-synuclein dimers.Biopolymers · 2016Article
- Article
- Probing of Amyloid Aβ (14-23) Trimers by Single-Molecule Force Spectroscopy.Jacobs journal of molecular and translational medicine · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Misfolding and subsequent aggregation of alpha-synuclein (α-Syn) protein are critically involved in the development of several neurodegenerative diseases, including Parkinson's disease (PD). Three familial single point mutations, A30P, E46K, and A53T, correlate with early onset PD; however, the molecular mechanism of the effects of these mutations on the structural properties of α-Syn and its propensity to misfold remains unclear. Here, we address this issue utilizing a single molecule AFM force spectroscopy approach in which structural details of dimers formed by all four variants of α-Syn are characterized. Analysis of the force spectroscopy data reflecting contour length distribution for α-Syn dimer dissociation suggests that multiple segments are involved in the assembly of the dimer. The interactions are not limited to the central nonamyloid-beta component (NAC) of the protein but rather expand beyond this segment. All three mutations alter the protein's folding and interaction patterns affecting interactions far beyond their immediate locations. Implementation of these findings to our understanding of α-Syn aggregation pathways is discussed.
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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.