ArticleACS chemical neuroscience2018
Alpha Synuclein Fibrils Contain Multiple Binding Sites for Small Molecules.
Article in ACS chemical neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 84 citations in OpenAlex.
- QSAR-Guided Virtual Screening and Molecular Dynamics Reveal Olaparib as a Repurposing Lead Against α-Synuclein Aggregation.International journal of molecular sciences · 2026Article
- A Structure-Activity Relationship Study of Alpha Synuclein PET Radiotracer M503-1619.Molecules (Basel, Switzerland) · 2026Article
- PET imaging of alpha-synuclein: from radiotracer design through in vitro and in vivo translation.European journal of nuclear medicine and molecular imaging · 2026Review
- Machine learning prediction of multiple distinct high-affinity chemotypes for α-synuclein fibrils.Chemical communications (Cambridge, England) · 2026Article
- Nuclear Medicine Imaging Biomarkers in Parkinson's Disease: Past, Present, and Future Directions.Medical sciences (Basel, Switzerland) · 2025Review
- Interactions of Neurodegenerative Disease Positron Emission Tomography Imaging Probe Candidates with the C-Terminus of α-Synuclein Fibrils.Chembiochem : a European journal of chemical biology · 2025Article
- Genetic code expansion and enzymatic modifications as accessible methods for studying site-specific post-translational modifications of alpha-synuclein and tau.Protein science : a publication of the Protein Society · 2025Article
- Article
- In Vitro Evaluation of Amide-Linked Coumarin Scaffolds for the Inhibition of α‑Synuclein and Tau Aggregation.ACS omega · 2025Article
- Advances in PET imaging of protein aggregates associated with neurodegenerative disease.Nature reviews. Neurology · 2025Review
- In silico identification of substrate-binding sites in type-1A α-synuclein amyloids.Biophysical journal · 2025Article
- Detecting alpha-synuclein aggregates with small molecules on single-molecule array.Chemical science · 2025Article
- Discovery ofCells · 2025Article
- Development of Positron Emission Tomography Radiotracers for Imaging α-Synuclein Aggregates.Cells · 2025Review
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Review
- Strategic Modulation of Polarity and Viscosity Sensitivity of Bimane Molecular Rotor-Based Fluorophores for Imaging α-Synuclein.Journal of the American Chemical Society · 2025Article
- Strategies of positron emission tomography (PET) tracer development for imaging of tau and α-synuclein in neurodegenerative disorders.RSC medicinal chemistry · 2025Review
- Identification and In Vitro and In Vivo Characterization of KAC-50.1 as a Potential α-Synuclein PET Radioligand.ACS chemical neuroscience · 2024Article
- Exploring the Potential of Biomimetic Peptides in Targeting Fibrillar and Filamentous Alpha-Synuclein-An In Silico and Experimental Approach to Parkinson's Disease.Biomimetics (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
Abstract
The fibrillary aggregation of the protein alpha synuclein (Asyn) is a hallmark of Parkinson's disease, and the identification of small molecule binding sites on fibrils is essential to the development of diagnostic imaging probes. A series of molecular modeling, photoaffinity labeling, mass spectrometry, and radioligand binding studies were conducted on Asyn fibrils. The results of these studies revealed the presence of three different binding sites within fibrillar Asyn capable of binding small molecules with moderate to high affinity. A knowledge of the amino acid residues in these binding sites will be important in the design of high affinity probes capable of imaging fibrillary species of Asyn.
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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.