ArticleAngewandte Chemie (International ed. in English)2018
Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE).
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 34 citations in OpenAlex.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- Evaluating the use of lanthanide containing dendrimers for solvent paramagnetic relaxation enhancement.Journal of biomolecular NMR · 2025Article
- Multistate Structure Determination and Dynamics Analysis Reveals a Unique Ubiquitin-Recognition Mechanism in Ubiquitin C-terminal Hydrolase.Journal of the American Chemical Society · 2025Article
- Conformational dynamics and multimodal interaction of Paxillin with the focal adhesion targeting domain.Science advances · 2025Article
- Conformational dynamics and multi-modal interaction of Paxillin with the Focal Adhesion Targeting Domain.bioRxiv : the preprint server for biology · 2025Article
- Quantitative Interpretation of Transverse Spin Relaxation by Translational Diffusion in Liquids.The journal of physical chemistry. B · 2025Article
- Analysis of the complex between MBD2 and the histone deacetylase core of NuRD reveals key interactions critical for gene silencing.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging.Biomolecules · 2022Review
- NMR illuminates intrinsic disorder.Current opinion in structural biology · 2021Review
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
- Lipid-nanodiscs formed by paramagnetic metal chelated polymer for fast NMR data acquisition.Biochimica et biophysica acta. Biomembranes · 2020Article
- Two Distinct Structures of Membrane-Associated Homodimers of GTP- and GDP-Bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement.Angewandte Chemie (International ed. in English) · 2020Article
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- A Double-Armed, Hydrophilic Transition Metal Complex as a Paramagnetic NMR Probe.Angewandte Chemie (International ed. in English) · 2019Review
- NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.Journal of biomolecular NMR · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Characterization of the conformational ensemble of disordered proteins is highly important for understanding protein folding and aggregation mechanisms, but remains a computational and experimental challenge owing to the dynamic nature of these proteins. New observables that can provide unique insights into transient residual structures in disordered proteins are needed. Here using denatured ubiquitin as a model system, NMR solvent paramagnetic relaxation enhancement (sPRE) measurements provide an accurate and highly sensitive probe for detecting low populations of residual structure in a disordered protein. Furthermore, a new ensemble calculation approach based on sPRE restraints in conjunction with residual dipolar couplings (RDCs) and small-angle X-ray scattering (SAXS) is used to define the conformational ensemble of disordered proteins at atomic resolution. The approach presented should be applicable to a wide range of dynamic macromolecules.
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.