ArticleProtein science : a publication of the Protein Society2018
FRETting about the affinity of bimolecular protein-protein interactions.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 14 citations in OpenAlex.
- A Single-Chain Variable Fragment Antibody Alleviates Inflammation and Apoptosis of Neurons by Inhibiting Tau Aggregation.Biomolecules · 2025Article
- Direct Quantification of Protein-Protein Interactions in Living Bacterial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Conjugation Chemistry Markedly Impacts Toxicity and Biodistribution of Targeted Nanoparticles, Mediated by Complement Activation.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Free Electron Density Gradients Enhanced Biosensor for Ultrasensitive and Accurate Affinity Assessment of the Immunotherapy Drugs.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals.Chemical reviews · 2024Review
- Chemical and Biological Strategies for Profiling Protein-Protein Interactions in Living Cells.Chemistry, an Asian journal · 2023Review
- Prediction of Protein-Protein Binding Affinities from Unbound Protein Structures.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Structure-guided evolution of Green2 toward photostability and quantum yield enhancement by F145Y substitution.Protein science : a publication of the Protein Society · 2020Article
- Advanced FRET normalization allows quantitative analysis of protein interactions including stoichiometries and relative affinities in living cells.Scientific reports · 2019Article
- Exploring Protein⁻Protein Interaction in the Study of Hormone-Dependent Cancers.International journal of molecular sciences · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Fluorescence resonance energy transfer (FRET) is a powerful tool to study macromolecular interactions such as protein-protein interactions (PPIs). Fluorescent protein (FP) fusions enable FRET-based PPI analysis of signaling pathways and molecular structure in living cells. Despite FRET's importance in PPI studies, FRET has seen limited use in quantifying the affinities of PPIs in living cells. Here, we have explored the relationship between FRET efficiency and PPI affinity over a wide range when expressed from a single plasmid system in Escherichia coli. Using live-cell microscopy and a set of 20 pairs of small interacting proteins, belonging to different structural folds and interaction affinities, we demonstrate that FRET efficiency can reliably measure the dissociation constant (K
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.