ArticleJournal of biomolecular NMR2014
Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes.
Article in Journal of biomolecular NMR, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Deuteration of proteins boosted by cell lysates: high-resolution amide and HMagnetic resonance (Gottingen, Germany) · 2024Article
- Review
- Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins.Solid state nuclear magnetic resonance · 2021Review
- Non-uniform sampling in quantitative assessment of heterogeneous solid-state NMR line shapes.Journal of biomolecular NMR · 2020Article
- Effect of Post-Translational Modifications and Mutations on Amyloid-β Fibrils Dynamics at N Terminus.Biophysical journal · 2019Article
- Deuteron Solid-State NMR Relaxation Measurements Reveal Two Distinct Conformational Exchange Processes in the Disordered N-Terminal Domain of Amyloid-β Fibrils.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- 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
- Ultrafast Hydrogen-Bonding Dynamics in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Methods (San Diego, Calif.) · 2018Review
- Basic experiments inMethods (San Diego, Calif.) · 2018Review
- Static solid-stateProgress in nuclear magnetic resonance spectroscopy · 2017Review
- Peptide and Protein Dynamics and Low-Temperature/DNP Magic Angle Spinning NMR.The journal of physical chemistry. B · 2017Article
- Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.Chemical physics letters · 2017Article
- Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Biophysical journal · 2016Article
- Enhancing NMR Sensitivity of Natural-Abundance Low-γ Nuclei by Ultrafast Magic-Angle-Spinning Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016Article
- Improving dipolar recoupling for site-specific structural and dynamics studies in biosolids NMR: windowed RN-symmetry sequences.Physical chemistry chemical physics : PCCP · 2016Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- A Novel High-Resolution and Sensitivity-Enhanced Three-Dimensional Solid-State NMR Experiment Under Ultrafast Magic Angle Spinning Conditions.Scientific reports · 2015Article
- Protein dynamics in the solid state from 2H NMR line shape analysis: a consistent perspective.The journal of physical chemistry. B · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregates formed by amyloidogenic peptides and proteins and reconstituted membrane protein preparations differ significantly in terms of the spectral quality that they display in solid-state NMR experiments. Structural heterogeneity and dynamics can both in principle account for that observation. This perspectives article aims to point out challenges and limitations, but also potential opportunities in the investigation of these systems.
Indexed as
Identifiers
24595988What 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.