ArticleChembiochem : a European journal of chemical biology2018
Super-resolution Imaging of Amyloid Structures over Extended Times by Using Transient Binding of Single Thioflavin T Molecules.
Article in Chembiochem : a European journal of chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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Who cites it
28 citing papers in PubMed.
- Single Fluorogens and Orientation-Localization Microscopy for Quantifying Chemical and Biomolecular Dynamics at the Nanoscale.Accounts of chemical research · 2026Article
- Seeing the Unseen: Super-Resolution Microscopy in Protein Aggregation Research.Chemical & biomedical imaging · 2026Review
- Transient binding facilitates super-resolution imaging of functional amyloid fibrils on living bacteria.Protein science : a publication of the Protein Society · 2026Article
- Visualizing liquid-liquid phase separation and protein aggregates.Communications chemistry · 2025Review
- Leveraging bioorthogonal conjugation for alpha synuclein fibril surveillance.bioRxiv : the preprint server for biology · 2025Article
- A Direct Relationship Between 'Blood Stasis' and Fibrinaloid Microclots in Chronic, Inflammatory, and Vascular Diseases, and Some Traditional Natural Products Approaches to Treatment.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Fluorescent Particles Based on Aggregation-Induced Emission for Optical Diagnostics of the Central Nervous System.Research (Washington, D.C.) · 2025Review
- Single-fluorogen imaging reveals distinct environmental and structural features of biomolecular condensates.Nature physics · 2025Article
- Single-molecule orientation-localization microscopy: Applications and approaches.Quarterly reviews of biophysics · 2024Review
- POLCAM: instant molecular orientation microscopy for the life sciences.Nature methods · 2024Article
- Article
- Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024Article
- Single-Molecule Orientation Imaging Reveals the Nano-Architecture of Amyloid Fibrils Undergoing Growth and Decay.Nano letters · 2024Article
- Single-Molecule Orientation Imaging Reveals the Nano-Architecture of Amyloid Fibrils Undergoing Growth and Decay.bioRxiv : the preprint server for biology · 2024Article
- Resolving the Nanoscale Structure of β-Sheet Peptide Self-Assemblies Using Single-Molecule Orientation-Localization Microscopy.ACS nano · 2024Article
- Beyond DNA: new probes for PAINT super-resolution microscopy.Chemical communications (Cambridge, England) · 2023Review
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Small soluble α-synuclein aggregates are the toxic species in Parkinson's disease.Nature communications · 2022Article
- Super-resolution microscopy: a closer look at synaptic dysfunction in Alzheimer disease.Nature reviews. Neuroscience · 2021Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Oligomeric amyloid structures are crucial therapeutic targets in Alzheimer's and other amyloid diseases. However, these oligomers are too small to be resolved by standard light microscopy. We have developed a simple and versatile tool to image amyloid structures by using thioflavin T without the need for covalent labeling or immunostaining. The dynamic binding of single dye molecules generates photon bursts that are used for fluorophore localization on a nanometer scale. Thus, photobleaching cannot degrade image quality, allowing for extended observation times. Super-resolution transient amyloid binding microscopy promises to directly image native amyloid by using standard probes and record amyloid dynamics over minutes to days. We imaged amyloid fibrils from multiple polypeptides, oligomeric, and fibrillar structures formed during different stages of amyloid-β aggregation, as well as the structural remodeling of amyloid-β fibrils by the compound epi-gallocatechin gallate.
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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.