ArticleMethods in molecular biology (Clifton, N.J.)2015
Bioluminescence resonance energy transfer to detect protein-protein interactions in live cells.
Article in Methods in molecular biology (Clifton, N.J.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 38 citations in OpenAlex.
- Functional methods for evaluating the efficacy of retinal optogenetic therapy for vision restoration.Frontiers in neuroscience · 2026Review
- A high-throughput screening approach to discover potential colorectal cancer chemotherapeutics: repurposing drugs to identify novel disruptors of 14-3-3 proteins.Cell death & disease · 2025Article
- Signal Transduction Strategies for DNAzyme-Based Sensing and Imaging of Metal Ions in Cells andChemical & biomedical imaging · 2025Review
- Article
- Exploiting Cell-Based Assays to Accelerate Drug Development for G Protein-Coupled Receptors.International journal of molecular sciences · 2024Review
- Ratiometric Detection of ZnChemistry (Basel, Switzerland) · 2023Article
- Optimization of BRET saturation assays for robust and sensitive cytosolic protein-protein interaction studies.Scientific reports · 2022Article
- Review
- Genetically encoded fluorescent tools: Shining a little light on ER-to-Golgi transport.Free radical biology & medicine · 2022Review
- Molecular insights into mechanisms of GPCR hijacking byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Differential Involvement of ACKR3 C-Tail in β-Arrestin Recruitment, Trafficking and Internalization.Cells · 2021Article
- Designing Chimeric Molecules for Drug Discovery by Leveraging Chemical Biology.Journal of medicinal chemistry · 2020Review
- Genetic Analysis of Rare Human Variants of Regulators of G Protein Signaling Proteins and Their Role in Human Physiology and Disease.Pharmacological reviews · 2018Review
- Molecular Evidence of Adenosine Deaminase Linking Adenosine AFrontiers in pharmacology · 2018Article
- RGS14 regulates the lifetime of GPharmacology research & perspectives · 2016Article
- Current Approaches Toward Quantitative Mapping of the Interactome.Frontiers in genetics · 2016Article
- Human genetic variants disrupt RGS14 nuclear shuttling and regulation of LTP in hippocampal neurons.The Journal of biological chemistryArticle
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 2 institutions in 1 country.
Funding
Abstract
Bioluminescence resonance energy transfer (BRET) is a valuable tool to detect protein-protein interactions. BRET utilizes bioluminescent and fluorescent protein tags with compatible emission and excitation properties, making it possible to examine resonance energy transfer when the tags are in close proximity (<10 nm) as a typical result of protein-protein interactions. Here we describe a protocol for detecting BRET from two known protein binding partners (Gαi1 and RGS14) in HEK 293 cells using Renilla luciferase and yellow fluorescent protein tags. We discuss the calculation of the acceptor/donor ratio as well as net BRET and demonstrate that BRET can be used as a platform to investigate the regulation of protein-protein interactions in live cells in real time.
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.