ArticleJournal of biomolecular NMR2017
Line-Broadening in Low-Temperature Solid-State NMR Spectra of Fibrils.
Article in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 32 citations in OpenAlex.
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- 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
- Resolution in cryogenic solid state NMR: Challenges and solutions.Protein science : a publication of the Protein Society · 2024Review
- Fast Magic-Angle-Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid C-Terminal Domain.Angewandte Chemie (International ed. in English) · 2022Article
- DNP-enhanced solid-state NMR spectroscopy of chromatin polymers.Journal of magnetic resonance open · 2022Article
- Transient RNA Interactions Leave a Covalent Imprint on a Viral Capsid Protein.Journal of the American Chemical Society · 2022Article
- Nucleic acid-protein interfaces studied by MAS solid-state NMR spectroscopy.Journal of structural biology: X · 2022Article
- Prion Amyloid Polymorphs - The Tag Might Change It All.Frontiers in molecular biosciences · 2020Article
- Solid-state NMR reveals a comprehensive view of the dynamics of the flexible, disordered N-terminal domain of amyloid-β fibrils.The Journal of biological chemistry · 2019Article
- Flexible-to-rigid transition is central for substrate transport in the ABC transporter BmrA fromCommunications biology · 2019Article
- High-resolution NMR studies of antibiotics in cellular membranes.Nature communications · 2018Article
- Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Methods (San Diego, Calif.) · 2018Article
- N,N-Diethylmethylamine as lineshape standard for NMR above 130 K.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- NMR Signal Quenching from Bound Biradical Affinity Reagents in DNP Samples.The journal of physical chemistry. B · 2017Article
- Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Solid state nuclear magnetic resonance · 2017Review
- Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.Journal of biomolecular NMR · 2017Article
- New NMR tools for protein structure and function: Spin tags for dynamic nuclear polarization solid state NMR.Archives of biochemistry and biophysics · 2017Review
- Efficient assignment and NMR analysis of an intact virus using sequential side-chain correlations and DNP sensitization.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Hexagonal ice in pure water and biological NMR samples.Journal of biomolecular NMR · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The temperature-dependent resonance-line broadening of HET-s(218-289) in its amyloid form is investigated in the range between 110 K and 280 K. Significant differences are observed between residues in the structured hydrophobic triangular core, which are broadened the least and can be detected down to 100 K, and in the solvent-exposed parts, which are broadened the most and often disappear from the observed spectrum around 200 K. Below the freezing of the bulk water, around 273 K, the protein fibrils are still surrounded by a layer of mobile water whose thickness decreases with temperature, leading to drying out of the 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.