ArticleNano letters2014
Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.
Article in Nano letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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
67 citing papers in PubMed.
- Seeing the Unseen: Super-Resolution Microscopy in Protein Aggregation Research.Chemical & biomedical imaging · 2026Review
- High-speed atomic force microscopy reveals a surface-catalyzed elongation mechanism of the fungal functional amyloid hydrophobin RolA.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.BBA advances · 2026Review
- Visualizing liquid-liquid phase separation and protein aggregates.Communications chemistry · 2025Review
- Single-fibril Förster resonance energy transfer imaging and deep learning reveal concentration dependence of amyloid β 42 aggregation pathways.PNAS nexus · 2025Article
- Super-resolution microscopy for structural biology.Nature methods · 2025Review
- Impact of α-synuclein fibril structure on seeding activity in experimental models of Parkinson's disease.NPJ Parkinson's disease · 2025Article
- Bacterial Amyloids as Hubs for Nucleic Acid Interactions: Implications and Mechanisms.International journal of molecular sciences · 2025Review
- Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024Review
- In cell NMR reveals cells selectively amplify and structurally remodel amyloid fibrils.bioRxiv : the preprint server for biology · 2024Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Direct Observation of Seeded Conformational Conversion of hIAPPJournal of chemical information and modeling · 2023Article
- Distinct growth regimes of α-synuclein amyloid elongation.Biophysical journal · 2023Article
- Time-Resolved In Situ AFM Measurement of Growth Rates of Aβ40 Fibrils.Methods in molecular biology (Clifton, N.J.) · 2023Article
- De novo designed protein inhibitors of amyloid aggregation and seeding.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Direct observation of heterogeneous formation of amyloid spherulites in real-time by super-resolution microscopy.Communications biology · 2022Article
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Using transient equilibria (TREQ) to measure the thermodynamics of slowly assembling supramolecular systems.Science advances · 2022Article
- Molecular insights into α-synuclein interaction with individual human core histones, linker histone, and dsDNA.Protein science : a publication of the Protein Society · 2021Article
- Selectivity of Lewy body protein interactions along the aggregation pathway of α-synuclein.Communications biology · 2021Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The self-assembly of normally soluble proteins into fibrillar amyloid structures is associated with a range of neurodegenerative disorders, such as Parkinson's and Alzheimer's diseases. In the present study, we show that specific events in the kinetics of the complex, multistep aggregation process of one such protein, α-synuclein, whose aggregation is a characteristic hallmark of Parkinson's disease, can be followed at the molecular level using optical super-resolution microscopy. We have explored in particular the elongation of preformed α-synuclein fibrils; using two-color single-molecule localization microscopy we are able to provide conclusive evidence that the elongation proceeds from both ends of the fibril seeds. Furthermore, the technique reveals a large heterogeneity in the growth rates of individual fibrils; some fibrils exhibit no detectable growth, whereas others extend to more than ten times their original length within hours. These large variations in the growth kinetics can be attributed to fibril structural polymorphism. Our technique offers new capabilities in the study of amyloid growth dynamics at the molecular level and is readily translated to the study of the self-assembly of other nanostructures.
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.