ArticleBiophysical journal2014
Type-3 BRET, an improved competition-based bioluminescence resonance energy transfer assay.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Oligomerization of yeast α-factor receptor detected by fluorescent energy transfer between ligands.Biophysical journal · 2021Article
- Third-Party Capture of Elusive GPCR Dimers.Biophysical journal · 2019Article
- Constraints on GPCR Heterodimerization Revealed by the Type-4 Induced-Association BRET Assay.Biophysical journal · 2019Article
- Receptor Quaternary Organization Explains G Protein-Coupled Receptor Family Structure.Cell reports · 2017Article
- Conformational biosensors reveal allosteric interactions between heterodimeric AT1 angiotensin and prostaglandin F2α receptors.The Journal of biological chemistry · 2017Article
- Referenced Single-Molecule Measurements Differentiate between GPCR Oligomerization States.Biophysical journal · 2015Article
- BRET evidence that β2 adrenergic receptors do not oligomerize in cells.Scientific reports · 2015Article
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.
Funding
Abstract
We show that in conventional, competition-based bioluminescence resonance energy transfer (BRET) assays of membrane protein stoichiometry, the presence of competitors can alter tagged-protein density and artifactually reduce energy transfer efficiency. A well-characterized monomeric type I membrane protein, CD86, and two G protein-coupled receptors β2AR and mCannR2, all of which behave as dimers in these conventional assays, exhibit monomeric behavior in an improved competition-based type-3 BRET assay designed to circumvent such artifacts.
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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.