ArticlePhysical chemistry chemical physics : PCCP2019
Time-resolved multirotational dynamics of single solution-phase tau proteins reveals details of conformational variation.
Article in Physical chemistry chemical physics : PCCP, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
The trial behind it
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
12 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Rational Modulation of Liquid-Liquid Phase Separation Offers Novel Ways to Combat Tauopathies.International journal of molecular sciences · 2025Review
- Evidence of a Three-State Mechanism in DNA Hairpin Folding.Journal of the American Chemical Society · 2025Article
- Quantifying Microsecond Solution-Phase Conformational Dynamics of a DNA Hairpin at the Single-Molecule Level.ACS physical chemistry Au · 2024Article
- Strategies for Overcoming the Single-Molecule Concentration Barrier.ACS measurement science au · 2023Review
- Investigation of the Structure of Full-Length Tau Proteins with Coarse-Grained and All-Atom Molecular Dynamics Simulations.ACS chemical neuroscience · 2023Article
- The Role of Post-Translational Modifications on the Structure and Function of Tau Protein.Journal of molecular neuroscience : MN · 2022Review
- The Structure Biology of Tau and Clue for Aggregation Inhibitor Design.The protein journal · 2021Review
- Protein Aggregation Landscape in Neurodegenerative Diseases: Clinical Relevance and Future Applications.International journal of molecular sciences · 2021Review
- The structure and phase of tau: from monomer to amyloid filament.Cellular and molecular life sciences : CMLS · 2021Review
- Optical monitoring of polymerizations in droplets with high temporal dynamic range.Chemical science · 2020Article
- Interferometric Scattering Enables Fluorescence-Free Electrokinetic Trapping of Single Nanoparticles in Free Solution.Nano letters · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Intrinsically disordered proteins (IDPs) are crucial to many cellular processes and have been linked to neurodegenerative diseases. Single molecules of tau, an IDP associated with Alzheimer's disease, are trapped in solution using a microfluidic device, and a time-resolved fluorescence anisotropy decay is recorded for each molecule. Multiple rotational components are resolved and a novel k-means algorithm is used to sort the molecules into two families of conformations. Differences in rotational dynamics suggest a change in the rigidity and steric hindrance surrounding a sequence (306VQIVYK311) which is central to paired helical filament formation. This single-molecule approach can be applied to other IDPs to resolve heterogeneous populations and underlying differences in conformational dynamics.
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What OpenQuestion holds
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.