ArticleAssay and drug development technologies2011
Fluorescence polarization screening for allosteric small molecule ligands of the cholecystokinin receptor.
Article in Assay and drug development technologies, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Biophysical screening methods for extracellular domain peptide receptors, application to natriuretic peptide receptor C ligands.Chemical biology & drug design · 2019Article
- Cholecystokinin-induced satiety, a key gut servomechanism that is affected by the membrane microenvironment of this receptor.International journal of obesity supplements · 2016Review
- Fluorescence- and bioluminescence-based approaches to study GPCR ligand binding.British journal of pharmacology · 2016Review
- Fluorescent approaches for understanding interactions of ligands with G protein coupled receptors.Biochimica et biophysica acta · 2014Review
- Identification of influenza endonuclease inhibitors using a novel fluorescence polarization assay.ACS chemical biology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The success in screening for drug candidates is highly dependent on the power of the strategy implemented. In this work, we report and characterize a novel fluorescent benzodiazepine antagonist of the type 1 cholecystokinin receptor (3-(3-(7-fluoro-1-(2-isopropyl(4-methoxyphenyl)amino)-2-oxoethyl)-2,4-dioxo-5-phenyl-2,3,4,5-tetrahydro-1H-benzo[b][1,4]-diazepin-3-yl)ureido)benzoic acid) that can be used as a receptor ligand in a fluorescence polarization assay, which is ideally suited for the identification of small molecule allosteric modulators of this physiologically important receptor. By binding directly to the small molecule-docking region within the helical bundle of this receptor, this indicator can be displaced by many small molecule candidate drugs, even those that might not affect the binding of an orthosteric cholecystokinin-like peptide ligand. The biological, pharmacological, and fluorescence properties of this reagent are described, and proof-of-concept is provided in a fluorescence polarization assay utilizing this fluorescent benzodiazepine ligand.
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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.