ArticleNature protocols2011
Analysis of protein-ligand interactions by fluorescence polarization.
Article in Nature protocols, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers, 2 of them syntheses that pooled it.
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
175 citing papers in PubMed, 2 syntheses or guidelines pooled it, 348 citations in OpenAlex.
- An Experimental Framework for Developing Point-of-Need Biosensors: Connecting Bio-Layer Interferometry and Electrochemical Impedance Spectroscopy.Biosensors · 2022Pooled it
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- Methods to Study the Molecular Mechanism and Drive the Design of Protein Degraders.Chemical reviews · 2026Review
- Discovery of SHANK1-PDZ Peptide-Fragment Inhibitors Using a Dynamic Ligation Screening Strategy.Biochemistry · 2026Article
- A High-throughput Fluorescence Polarization Assay for Screening Sirtuin Inhibitors.bioRxiv : the preprint server for biology · 2026Article
- Structural and Kinetic Basis for the Rational Design of Next-Generation β-Lactamase Inhibitors.Journal of medicinal chemistry · 2026Article
- Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.bioRxiv : the preprint server for biology · 2026Article
- Native mass spectrometry enabled by infrared matrix-assisted laser desorption electrospray ionization for rapid measurement of protein-ligand biophysical parameters.Analytical and bioanalytical chemistry · 2026Article
- A Site-Specific Self-Association of a Protein Hub Drives Its Phase Separation.ACS chemical biology · 2026Article
- Fluorescence Anisotropy Applied to Measure Aptamer-Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Role of Surfactants in Stabilizing Fluorescence Anisotropy for Protein-Aptamer Binding Affinity Measurements.Biosensors · 2025Article
- Coacervates of Lactoferrin with Resistant Dextrin via Noncovalent Interaction for Enhanced Thermal Stability, Interface Characteristics and Docosahexaenoic Acid (DHA) Encapsulation.Food science of animal resources · 2025Article
- Accurate and Rapid Ranking of Protein-Ligand Binding Affinities Using Density Matrix Fragmentation and Physics-Informed Machine Learning Dispersion Potentials.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Rapid clearance of achiral small-molecule drugs using de novo-designed proteins and their cyclic and mirror-image variants.Nature biomedical engineering · 2025Article
- Article
- Antigenic homology between mouse spermatozoa and Vibrio cholerae: in-silico, in-vitro, and in-vivo evidence for immune-mediated infertility.Archives of microbiology · 2025Article
- Structural basis for saxitoxin congener binding and neutralization by anuran saxiphilins.Nature communications · 2025Article
115 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 2 institutions in 2 countries.
Funding
Abstract
Quantification of the associations between biomolecules is required both to predict and understand the interactions that underpin all biological activity. Fluorescence polarization (FP) provides a nondisruptive means of measuring the association of a fluorescent ligand with a larger molecule. We describe an FP assay in which binding of fluorescein-labeled inositol 1,4,5-trisphosphate (IP(3)) to N-terminal fragments of IP(3) receptors can be characterized at different temperatures and in competition with other ligands. The assay allows the standard Gibbs free energy (ΔG°), enthalpy (ΔH°) and entropy (ΔS°) changes of ligand binding to be determined. The method is applicable to any purified ligand-binding site for which an appropriate fluorescent ligand is available. FP can be used to measure low-affinity interactions in real time without the use of radioactive materials, it is nondestructive and, with appropriate care, it can resolve ΔH° and ΔS°. The first part of the protocol, protein preparation, may take several weeks, whereas the FP measurements, once they have been optimized, would normally take 1-6 h.
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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.