<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Field DH</submitter><funding>University of Leeds</funding><funding>Leverhulme Trust</funding><funding>Royal Society</funding><funding>Wellcome Trust</funding><funding>Engineering and Physical Sciences Research Council</funding><pagination>216-222</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9994102</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>4(3)</volume><pubmed_abstract>Fluorescent ligands for G-protein coupled receptors (GPCRs) are valuable tools for studying the expression, pharmacology and modulation of these therapeutically important proteins in living cells. Here we report a fluorescent photoaffinity probe for Formyl peptide receptor 1 (FPR1), a critical component of the innate immune response to bacterial infection and a promising target in inflammatory diseases. We demonstrate that the probe binds and covalently crosslinks to FPR1 with good specificity at nanomolar concentrations in living cells and is a useful tool for visualisation and characterisation of this receptor.</pubmed_abstract><journal>RSC chemical biology</journal><pubmed_title>A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells.</pubmed_title><pmcid>PMC9994102</pmcid><funding_grant_id>RG160914</funding_grant_id><funding_grant_id>1930246</funding_grant_id><funding_grant_id>WT104918MA</funding_grant_id><funding_grant_id>RPG-2018-030</funding_grant_id><pubmed_authors>Wright MH</pubmed_authors><pubmed_authors>Field DH</pubmed_authors><pubmed_authors>White JS</pubmed_authors><pubmed_authors>Warriner SL</pubmed_authors></additional><is_claimable>false</is_claimable><name>A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells.</name><description>Fluorescent ligands for G-protein coupled receptors (GPCRs) are valuable tools for studying the expression, pharmacology and modulation of these therapeutically important proteins in living cells. Here we report a fluorescent photoaffinity probe for Formyl peptide receptor 1 (FPR1), a critical component of the innate immune response to bacterial infection and a promising target in inflammatory diseases. We demonstrate that the probe binds and covalently crosslinks to FPR1 with good specificity at nanomolar concentrations in living cells and is a useful tool for visualisation and characterisation of this receptor.</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Mar</publication><modification>2026-05-28T22:45:22.667Z</modification><creation>2025-04-04T20:21:47.736Z</creation></dates><accession>S-EPMC9994102</accession><cross_references><pubmed>36908701</pubmed><doi>10.1039/d2cb00199c</doi></cross_references></HashMap>