ArticleBiophysical journal2012
Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Single molecule imaging of protein aggregation in Dementia: Methods, insights and prospects.Neurobiology of disease · 2021Review
- Mapping Surface Hydrophobicity of α-Synuclein Oligomers at the Nanoscale.Nano letters · 2018Article
- Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.Chembiochem : a European journal of chemical biology · 2018Article
- 2D polarization imaging as a low-cost fluorescence method to detect α-synuclein aggregation ex vivo in models of Parkinson's disease.Communications biology · 2018Article
- Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation.Biophysical journal · 2017Article
- Polarized super-resolution structural imaging inside amyloid fibrils using Thioflavine T.Scientific reports · 2017Article
- Vertebrate food products as a potential source of prion-like α-synuclein.NPJ Parkinson's disease · 2017Review
- Probing amyloid protein aggregation with optical superresolution methods: from the test tube to models of disease.Neurophotonics · 2016Article
- From single-molecule spectroscopy to super-resolution imaging of the neuron: a review.Methods and applications in fluorescence · 2016Review
- Direct Observation of α-Synuclein Amyloid Aggregates in Endocytic Vesicles of Neuroblastoma Cells.PloS one · 2016Article
- Super-resolution fluorescence of huntingtin reveals growth of globular species into short fibers and coexistence of distinct aggregates.ACS chemical biology · 2014Article
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Direct observation of heterogeneous amyloid fibril growth kinetics via two-color super-resolution microscopy.Nano letters · 2014Article
- Super-resolution fluorescence imaging with single molecules.Current opinion in structural biology · 2013Review
- Superresolution imaging of amyloid fibrils with binding-activated probes.ACS chemical neuroscience · 2013Article
- α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.Molecular neurobiology · 2013Review
- Cellular inclusion bodies of mutant huntingtin exon 1 obscure small fibrillar aggregate species.Scientific reports · 2012Article
- The Binding of BF-227-Like Benzoxazoles to Human α-Synuclein and Amyloid β Peptide Fibrils.Molecular imagingArticle
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The morphological features of α-synuclein (AS) amyloid aggregation in vitro and in cells were elucidated at the nanoscale by far-field subdiffraction fluorescence localization microscopy. Labeling AS with rhodamine spiroamide probes allowed us to image AS fibrillar structures by fluorescence stochastic nanoscopy with an enhanced resolution at least 10-fold higher than that achieved with conventional, diffraction-limited techniques. The implementation of dual-color detection, combined with atomic force microscopy, revealed the propagation of individual fibrils in vitro. In cells, labeled protein appeared as amyloid aggregates of spheroidal morphology and subdiffraction sizes compatible with in vitro supramolecular intermediates perceived independently by atomic force microscopy and cryo-electron tomography. We estimated the number of monomeric protein units present in these minute structures. This approach is ideally suited for the investigation of the molecular mechanisms of amyloid formation both in vitro and in the cellular milieu.
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