ArticleJournal of the American Chemical Society2017
Water Distribution, Dynamics, and Interactions with Alzheimer's β-Amyloid Fibrils Investigated by Solid-State NMR.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 94 citations in OpenAlex.
- T1 mapping in Alzheimer's disease: a quantitative MRI study with amyloid-PET correlation.European radiology experimental · 2026Article
- Hydration water dynamics in amyloid-β aggregates using deuterium and oxygen-17 solid-state NMR spectroscopy.The Journal of chemical physics · 2026Article
- Dynamics studies of side-chains and hydration shells in amyloid-β fibrils using deuterium and oxygen-17 solid-state NMR.Methods in enzymology · 2026Review
- Multi-mode water dynamics in hydration shells of villin headpiece subdomain protein in the solid state using deuterium and oxygen-17 NMR spectroscopy.The Journal of chemical physics · 2025Article
- Tracing the aggregation pathway of the scaffold protein DISC1: Structural implications for chronic mental illnesses.Journal of structural biology: X · 2025Article
- Solid-state NMR protocols for unveiling dynamics and (drug) interactions of membrane-bound proteins.Protein science : a publication of the Protein Society · 2025Article
- Pseudo-Phosphorylated Tau Forms Paired Helical Filaments in the Presence of High-Curvature Cholesterol-Containing Lipid Membranes.Journal of the American Chemical Society · 2025Article
- Investigation of biomolecular dynamics by sensitivity-enhancedJournal of magnetic resonance open · 2024Article
- Selective Detection of Intermediate-Amplitude Motion by Solid-State NMR.The journal of physical chemistry. B · 2024Article
- From Fundamental Amyloid Protein Self-Assembly to Development of Bioplastics.Biomacromolecules · 2024Review
- Rapid Determination of the Topology of Oligomeric α-Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR.The journal of physical chemistry. B · 2023Article
- The role of water in reactions catalysed by hydrolases under conditions of molecular crowding.Biophysical reviews · 2023Review
- Amyloid fibril structures of tau: Conformational plasticity of the second microtubule-binding repeat.Science advances · 2023Article
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- Water Dynamics in Highly Concentrated Protein Systems-Insight from Nuclear Magnetic Resonance Relaxometry.International journal of molecular sciences · 2023Article
- EMBER multi-dimensional spectral microscopy enables quantitative determination of disease- and cell-specific amyloid strains.bioRxiv : the preprint server for biology · 2023Article
- The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.Nature communications · 2022Article
- Microtubule-binding core of the tau protein.Science advances · 2022Article
- Article
- Soluble TREM2 inhibits secondary nucleation of Aβ fibrillization and enhances cellular uptake of fibrillar Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Water is essential for protein folding and assembly of amyloid fibrils. Internal water cavities have been proposed for several amyloid fibrils, but no direct structural and dynamical data have been reported on the water dynamics and site-specific interactions of water with the fibrils. Here we use solid-state NMR spectroscopy to investigate the water interactions of several Aβ40 fibrils.
Indexed as
Identifiers
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.