ArticleACS applied materials & interfaces2025
Molecular Rotors Detect the Formation and Conversion of α-Synuclein Oligomers.
Article in ACS applied materials & interfaces, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Synuclein is an intrinsically disordered protein that forms amyloids in Parkinson's disease. Currently, detection methods predominantly report on the formation of mature amyloids but are weakly sensitive to the early stage, toxic oligomers. Molecular rotors are fluorophores that sense changes in the viscosity of their local environment. Here, we monitor α-synuclein oligomer formation using the fluorescence lifetime of molecular rotors. We detect oligomer formation and conversion into amyloids for wild-type and two α-synuclein variants, the pathological mutant A30P and ΔP1 α-synuclein, which lacks a master regulator region of aggregation (residues 36-42). We report that A30P α-synuclein shows a rate of oligomer formation similar to that of wild-type α-synuclein, whereas ΔP1 α-synuclein shows delayed oligomer formation. Additionally, both variants demonstrate a slower conversion of oligomers into amyloids. Our method provides a quantitative approach to unveiling the complex mechanism of α-synuclein aggregation, which is key to understanding the pathology of Parkinson's disease.
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.