ArticleNature chemical biology2017
HTS-compatible FRET-based conformational sensors clarify membrane receptor activation.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed.
- Subtype-dependent arrestin engagement of the metabotropic glutamate receptors.Nature communications · 2026Article
- TR-FRET between engineered nanobodies reveals the existence of endogenous CXCR4 oligomers.Communications biology · 2025Article
- Steric disruption of EGFR oligomerization overcomes therapy resistance in non-small cell lung cancer.Science advances · 2025Article
- Article
- Allosteric targeted drug delivery for enhanced blood-brain barrier penetration via mimicking transmembrane domain interactions.Nature communications · 2025Article
- Structural basis of orientated asymmetry in a mGlu heterodimer.Nature communications · 2024Article
- Repurposing conformational changes in ANL superfamily enzymes to rapidly generate biosensors for organic and amino acids.Nature communications · 2023Article
- Concerted conformational changes control metabotropic glutamate receptor activity.Science advances · 2023Article
- Finding the Perfect Fit: Conformational Biosensors to Determine the Efficacy of GPCR Ligands.ACS pharmacology & translational science · 2022Review
- Nanobody-based sensors reveal a high proportion of mGlu heterodimers in the brain.Nature chemical biology · 2022Article
- Structural basis of the activation of metabotropic glutamate receptor 3.Cell research · 2022Article
- Article
- Frizzled BRET sensors based on bioorthogonal labeling of unnatural amino acids reveal WNT-induced dynamics of the cysteine-rich domain.Science advances · 2021Article
- Allosteric modulators enhance agonist efficacy by increasing the residence time of a GPCR in the active state.Nature communications · 2021Article
- Agonists and allosteric modulators promote signaling from different metabotropic glutamate receptor 5 conformations.Cell reports · 2021Article
- A nanobody activating metabotropic glutamate receptor 4 discriminates between homo- and heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Multiple GPCR Functional Assays Based on Resonance Energy Transfer Sensors.Frontiers in cell and developmental biology · 2021Review
- Illuminating the allosteric modulation of the calcium-sensing receptor.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Interrogating surfaceChemical science · 2020Article
- Nanoscale co-organization and coactivation of AMPAR, NMDAR, and mGluR at excitatory synapses.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell surface receptors represent a vast majority of drug targets. Efforts have been conducted to develop biosensors reporting their conformational changes in live cells for pharmacological and functional studies. Although Förster resonance energy transfer (FRET) appears to be an ideal approach, its use is limited by the low signal-to-noise ratio. Here we report a toolbox composed of a combination of labeling technologies, specific fluorophores compatible with time-resolved FRET and a novel method to quantify signals. This approach enables the development of receptor biosensors with a large signal-to-noise ratio. We illustrate the usefulness of this toolbox through the development of biosensors for various G-protein-coupled receptors and receptor tyrosine kinases. These receptors include mGlu, GABA
Indexed as
Identifiers
28135236What 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.