ArticleProceedings of the National Academy of Sciences of the United States of America2019
Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 103 citations in OpenAlex.
- From a prion seed to a tree of discoveries: Byron Caughey's RT-QuIC legacy in protein misfolding research.Acta neuropathologica · 2026Review
- Breaking hydrogen bond network enhances oxygenic photosynthesis of photosystem II.Fundamental research · 2026Article
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Digging into Soil: Effects of Soil Texture on RT-QuIC Performance for Environmental Prion Surveillance.Environmental science & technology · 2026Article
- Brain-Derived Extracellular Vesicle Subpopulations: from Bulk Measurements to Single-Entity Assays.JACS Au · 2026Review
- Evaluating the Role of α-Synuclein Seed Amplification as a Disease Progression Marker: Evidence and Uncertainties.Movement disorders clinical practice · 2026Article
- Evidence for different seeding activities of misfolded tau in classical and rapidly progressive Alzheimer's disease.Brain pathology (Zurich, Switzerland) · 2026Article
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Design of Tau Aggregation Inhibitors Using Iterative Machine Learning and a Polymorph-Specific Brain-Seeded Fibril Amplification Assay.Journal of the American Chemical Society · 2025Article
- Serial amplification of tau filaments using Alzheimer's brain homogenates and C322A or C322S recombinant tau.FEBS letters · 2025Article
- Biological definitions of synucleinopathies should be anchored in clinical trajectories and encompass the complex biology of the disease.Journal of Parkinson's disease · 2025Review
- Alpha-synuclein seeding amplification assays in Lewy body dementia: a brief review.Molecular neurodegeneration · 2025Review
- A same day α-synuclein RT-QuIC seed amplification assay for synucleinopathy biospecimens.Npj biosensing · 2025Article
- Tracking Prions by RT-QuIC: An Update.Sub-cellular biochemistry · 2025Review
- QuICSeedR: an R package for analyzing fluorophore-assisted seed amplification assay data.Bioinformatics (Oxford, England) · 2024Article
- Targeting Endogenous Tau in Seeded Tauopathy Models Inhibits Tau Spread.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- α-Synuclein seeding amplification assays for diagnosing synucleinopathies: an innovative tool in clinical implementation.Translational neurodegeneration · 2024Review
- Ultrasensitive detection of TDP-43 and amyloid-β protein aggregates using micelle-assisted seed amplification assay.Translational neurodegeneration · 2024Article
- Rapid and sensitive determination of residual prion infectivity from prion-decontaminated surfaces.mSphere · 2024Article
- Enhanced quantitation of pathological α-synuclein in patient biospecimens by RT-QuIC seed amplification assays.PLoS pathogens · 2024Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Recent work with prion diseases and synucleinopathies indicates that accurate diagnostic methods for protein-folding diseases can be based on the ultrasensitive, amplified measurement of pathological aggregates in biospecimens. A better understanding of the physicochemical factors that control the seeded polymerization of such aggregates, and their amplification in vitro, should allow improvements in existing assay platforms, as well as the development of new assays for other proteopathic aggregates. Here, we systematically investigated the effects of the ionic environment on the polymerization of tau, α-synuclein, and the prion protein (PrP) induced by aggregates in biospecimens. We screened salts of the Hofmeister series, a relative ordering of strongly and weakly hydrated salts that tend to precipitate or solubilize proteins. We found that sensitivities of tau-based assays for Alzheimer's seeds and PrP-based assays for prions were best in weakly hydrated anions. In contrast, we saw an inverse trend with different tau-based assays, improving detection sensitivity for progressive supranuclear palsy seeds by ≈10
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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.