ReviewBiochimica et biophysica acta2014
Fluorescent approaches for understanding interactions of ligands with G protein coupled receptors.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 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
43 citing papers in PubMed, 116 citations in OpenAlex.
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- Navigating Solute Carrier Transporters-A Comprehensive Review of Functionalized Small Molecule Probes for Target Identification and Characterization.Medicinal research reviews · 2026Review
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- Exploring anticancer activity of baicalin, naringenin, and noscapine via binding and inhibition of sphingosine kinase 1.3 Biotech · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Design, Synthesis, and Characterization of New δ Opioid Receptor-Selective Fluorescent Probes and Applications in Single-Molecule Microscopy of Wild-Type Receptors.Journal of medicinal chemistry · 2024Article
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- Development and Characterization of Potent Succinate Receptor Fluorescent Tracers.Journal of medicinal chemistry · 2023Article
- Small Molecule Tools to Study Cellular Target Engagement for the Intracellular Allosteric Binding Site of GPCRs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Qualitative Estimation of Protein-Ligand Complex Stability through Thermal Titration Molecular Dynamics Simulations.Journal of chemical information and modeling · 2022Article
- Insertion of Nanoluc into the Extracellular Loops as a Complementary Method To Establish BRET-Based Binding Assays for GPCRs.ACS pharmacology & translational science · 2022Article
- Strategies for Improving Bioavailability, Bioactivity, and Physical-Chemical Behavior of Curcumin.Molecules (Basel, Switzerland) · 2022Review
- An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins.Communications biology · 2022Article
- Intercellular Communication in the Central Nervous System as Deduced by Chemical Neuroanatomy and Quantitative Analysis of Images: Impact on Neuropharmacology.International journal of molecular sciences · 2022Review
- Oligomerization of yeast α-factor receptor detected by fluorescent energy transfer between ligands.Biophysical journal · 2021Article
- Environment-Sensitive Fluorescence of 7-Nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-Labeled Ligands for Serotonin Receptors.Molecules (Basel, Switzerland) · 2021Article
- Dielectric Spectroscopy Based Detection of Specific and Nonspecific Cellular Mechanisms.Sensors (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
G protein coupled receptors are responsible for a wide variety of signaling responses in diverse cell types. Despite major advances in the determination of structures of this class of receptors, the underlying mechanisms by which binding of different types of ligands specifically elicits particular signaling responses remain unclear. The use of fluorescence spectroscopy can provide important information about the process of ligand binding and ligand dependent conformational changes in receptors, especially kinetic aspects of these processes that can be difficult to extract from X-ray structures. We present an overview of the extensive array of fluorescent ligands that have been used in studies of G protein coupled receptors and describe spectroscopic approaches for assaying binding and probing the environment of receptor-bound ligands with particular attention to examples involving yeast pheromone receptors. In addition, we discuss the use of fluorescence spectroscopy for detecting and characterizing conformational changes in receptors induced by the binding of ligands. Such studies have provided strong evidence for diversity of receptor conformations elicited by different ligands, consistent with the idea that GPCRs are not simple on and off switches. This diversity of states constitutes an underlying mechanistic basis for biased agonism, the observation that different stimuli can produce different responses from a single receptor. It is likely that continued technical advances will allow fluorescence spectroscopy to play an important role in continued probing of structural transitions in G protein coupled receptors. This article is part of a Special Issue entitled: Structural and biophysical characterisation of membrane protein-ligand binding.
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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.