ArticlePloS one2014
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed.
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Microfluidic platform for understanding Parkinson's disease and α-synuclein conformation.Translational neurodegeneration · 2025Review
- Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Single-Molecule Insight Into α-Synuclein Fibril Structure and Mechanics Modulated by Chemical Compounds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Oligomeric and Fibrillar α-Synuclein Display Persistent Dynamics and Compressibility under Controlled Confinement.ACS chemical neuroscience · 2023Article
- Developments in Trapped Ion Mobility Mass Spectrometry to Probe the Early Stages of Peptide Aggregation.Journal of the American Society for Mass Spectrometry · 2023Article
- Quantifying Oligomer Populations in Real Time during Protein Aggregation Using Single-Molecule Mass Photometry.ACS nano · 2022Article
- New insights into the folding-unfolding mechanism and conformations of cytochrome C.Chemical science · 2022Article
- Brain region-specific susceptibility of Lewy body pathology in synucleinopathies is governed by α-synuclein conformations.Acta neuropathologica · 2022Article
- Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Synthesis runs counter to directional folding of a nascent protein domain.Nature communications · 2020Article
- Optical Tweezers Approaches for Probing Multiscale Protein Mechanics and Assembly.Frontiers in molecular biosciences · 2020Review
- Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- 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
- Size and topology modulate the effects of frustration in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Pre-aggregation kinetics and intermediates of α-synuclein monitored by the ESIPT probe 7MFE.European biophysics journal : EBJ · 2018Article
- Structural characteristics and membrane interactions of tandem α-synuclein oligomers.Scientific reports · 2018Article
- A scalable approach to the computation of invariant measures for high-dimensional Markovian systems.Scientific reports · 2018Article
- Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories.Nature communications · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Oligomeric aggregates are widely suspected as toxic agents in diseases caused by protein aggregation, yet they remain poorly characterized, partly because they are challenging to isolate from a heterogeneous mixture of species. We developed an assay for characterizing structure, stability, and kinetics of individual oligomers at high resolution and sensitivity using single-molecule force spectroscopy, and applied it to observe the formation of transient structured aggregates within single oligomers of α-synuclein, an intrinsically-disordered protein linked to Parkinson's disease. Measurements of the molecular extension as the proteins unfolded under tension in optical tweezers revealed that even small oligomers could form numerous metastable structures, with a surprisingly broad range of sizes. Comparing the structures formed in monomers, dimers and tetramers, we found that the average mechanical stability increased with oligomer size. Most structures formed within a minute, with size-dependent rates. These results provide a new window onto the complex α-synuclein aggregation landscape, characterizing the microscopic structural heterogeneity and kinetics of different pathways.
Indexed as
Identifiers
What OpenQuestion holds
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.