ArticleQuarterly reviews of biophysics2015
Visualizing transient dark states by NMR spectroscopy.
Article in Quarterly reviews of biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 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
113 citing papers in PubMed, 227 citations in OpenAlex.
- GDP-Loaded K-Ras Transiently Binds to Effector B-Raf RBD, Mirroring the Structure of the Active GTP-Loaded Complex.Journal of the American Chemical Society · 2026Article
- ONEST: a web-based platform for the rapid and robust analysis of protein excited states through CEST spectroscopy.Bioinformatics (Oxford, England) · 2026Article
- Resolving Conformational Heterogeneity in Intrinsically Disordered Proteins via Experimentally Guided Multi-Replica Simulations.bioRxiv : the preprint server for biology · 2026Article
- Beyond structures: solution NMR as the quantitative engine of integrated structural biology.Frontiers in molecular biosciences · 2026Review
- Kinetic Mechanism of Substoichiometric Inhibition of Huntingtin Exon-1 Protein Aggregation by Selenium Nanoparticles.Small science · 2025Article
- NMR methods for investigating functionally relevant biomolecular dynamics.Magnetic resonance letters · 2025Review
- Elucidating Surface Adsorption of Lithium Ions on Electrode Materials UsingJournal of the American Chemical Society · 2025Article
- Exploring the Frontiers of Computational NMR: Methods, Applications, and Challenges.Chemical reviews · 2025Review
- Evaluating the use of lanthanide containing dendrimers for solvent paramagnetic relaxation enhancement.Journal of biomolecular NMR · 2025Article
- Dynamics of hydrogen-bonded end groups in bulk polymers revealed by solid-state NMR spectroscopy relaxation dispersion experiments.Communications chemistry · 2025Article
- Unraveling structural transitions and kinetics along the fold-switching pathway of the RfaH C-terminal domain using exchange-based NMR.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Decoding chaperone complexes: Insights from NMR spectroscopy.Biophysics reviews · 2024Review
- A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular insights into the interaction between a disordered protein and a folded RNA.bioRxiv : the preprint server for biology · 2024Article
- An RNA excited conformational state at atomic resolution.Nature communications · 2023Article
- ColabFold predicts alternative protein structures from single sequences, coevolution unnecessary for AF-cluster.bioRxiv : the preprint server for biology · 2023Article
- Probing excited stateMethods (San Diego, Calif.) · 2023Article
- Studying micro to millisecond protein dynamics using simple amideJournal of biomolecular NMR · 2023Article
- Multi-Site Conformational Exchange in the Synthetic Neomycin-Sensing Riboswitch Studied byAngewandte Chemie (International ed. in English) · 2023Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Myriad biological processes proceed through states that defy characterization by conventional atomic-resolution structural biological methods. The invisibility of these 'dark' states can arise from their transient nature, low equilibrium population, large molecular weight, and/or heterogeneity. Although they are invisible, these dark states underlie a range of processes, acting as encounter complexes between proteins and as intermediates in protein folding and aggregation. New methods have made these states accessible to high-resolution analysis by nuclear magnetic resonance (NMR) spectroscopy, as long as the dark state is in dynamic equilibrium with an NMR-visible species. These methods - paramagnetic NMR, relaxation dispersion, saturation transfer, lifetime line broadening, and hydrogen exchange - allow the exploration of otherwise invisible states in exchange with a visible species over a range of timescales, each taking advantage of some unique property of the dark state to amplify its effect on a particular NMR observable. In this review, we introduce these methods and explore two specific techniques - paramagnetic relaxation enhancement and dark state exchange saturation transfer - in greater detail.
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.