ReviewBiochimica et biophysica acta2010
Molecular mechanism of Thioflavin-T binding to amyloid fibrils.
Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 703 papers.
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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.
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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.
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Who cites it
703 citing papers in PubMed, 2,132 citations in OpenAlex.
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- Dose-Dependent Influence of RBD-Derived Amyloidogenic Peptides on SARS-CoV-2 Infectivity: A Cautionary Tale for Antiviral Design.International journal of molecular sciences · 2026Article
- Fibrillation/defibrillation of myoglobin decorated with gold nanoparticles probed through nanometal surface energy transfer mechanism.RSC advances · 2026Article
- Ultrafast Charge Transfer Dynamics of Thioflavin T Probed by Time-Resolved Raman Spectroscopy.ACS physical chemistry Au · 2026Article
- Recent Advances in Organofluoroprobes for Brain Imaging: Progress, Challenges, and Future Directions.ACS pharmacology & translational science · 2026Review
- Protein disulfide isomerase dissolves and detoxifies oligomeric assemblies of amyloid beta peptide.FEBS letters · 2026Article
- Janus Polymeric Nanorods Inhibit human Amylin Oligomerization and Fibrillation for Potential Type 2 Diabetes Treatment.Small science · 2026Article
- Article
- A small molecule modulating heterogeneous amyloid-β isoforms improves cognitive and pathological outcomes in acute and 5XFAD Alzheimer's disease models.Alzheimer's research & therapy · 2026Article
643 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since its first description in 1959, the fluorescent dye Thioflavin-T (ThT) has become among the most widely used "gold standards" for selectively staining and identifying amyloid fibrils both in vivo and in vitro. The large enhancement of its fluorescence emission upon binding to fibrils makes ThT a particularly powerful and convenient tool. Despite its widespread use in clinical and basic science applications, the molecular mechanism for the ability of ThT to recognize diverse types of amyloid fibrils and for the dye's characteristic fluorescence has only begun to be elucidated. Here, we review recent progress in the understanding of ThT-fibril interactions at an atomic resolution. These studies have yielded important insights into amyloid structures and the processes of fibril formation, and they also offer guidance for designing the next generation of amyloid assembly diagnostics, inhibitors, and therapeutics.
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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.