{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T14:53:41Z","timestamp":1790952821765,"version":"4.1.0"},"reference-count":60,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2015,7,6]],"date-time":"2015-07-06T00:00:00Z","timestamp":1436140800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2015,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Retinoid X receptors (RXRs) play a role as master regulators because of their capacity to form heterodimers with other nuclear receptors (NRs). Accordingly, retinoid signaling is involved in multiple biologic processes, including development, cell differentiation, metabolism, and cell death. However, the role and function of RXRs in different heterodimer complexes remain unidentified, mainly because most RXR drugs (called rexinoids) are not selective of specific heterodimer complexes. The lack of selectivity strongly limits the use of rexinoids for specific therapeutic approaches. To better characterize rexinoids at specific NR complexes, we have developed and optimized luciferase (Luc) protein complementation (PCA)\u2010based bioluminescence resonance energy transfer (BRET) assays that can directly measure recruitment of a coactivator (CoA) motif fused to yellow fluorescent protein (YFP) by specific NR dimers. To validate the assays, we compared rexinoid modulation of CoA recruitment by the RXR homodimer and by the heterodimers Nur77\/RXR and Nurr1\/RXR. Results revealed that some rexinoids display selective CoA recruitment activities with homo\u2010 or heterodimer complexes. In particular, SR11237 (BMS649) has stronger potency for recruitment of CoA motif and transcriptional activity with the heterodimer Nur77\/RXR than other complexes. This technology should be useful in identifying new compounds with specificity for individual dimeric species formed by NRs.\u2014Giner, X. C., Cotnoir\u2010White, D., Mader, S., L\u00e9vesque, D. Selective ligand activity at Nur\/retinoid X receptor complexes revealed by dimer\u2010specific bioluminescence resonance energy transfer\u2010based sensors.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    29, 4256\u20104267 (2015).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.14-259804","type":"journal-article","created":{"date-parts":[[2015,7,6]],"date-time":"2015-07-06T23:00:28Z","timestamp":1436223628000},"page":"4256-4267","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["Selective ligand activity at Nur\/retinoid X receptor complexes revealed by dimer\u2010specific bioluminescence resonance energy transfer\u2010based sensors"],"prefix":"10.1096","volume":"29","author":[{"given":"Xavier 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