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RXRs: Collegial Partners | SpringerLink
Description:
Retinoid X Receptors (RXR) were initially identified as nuclear receptors binding with stereo-selectivity the vitamin A derivative 9-cis retinoic acid, although the relevance of this molecule as endogenous activator of RXRs is still elusive. Importantly, within the...
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Keywords {🔍}
pubmed, google, scholar, cas, receptor, nuclear, retinoid, central, receptors, acid, rxr, cell, biol, mol, retinoic, hormone, chem, nature, binding, thyroid, chambon, genes, cancer, evans, alpha, activation, desvergne, peroxisome, structure, heterodimers, ligand, transcriptional, human, liu, heyman, res, endocrinol, function, chapter, proliferatoractivated, mangelsdorf, chen, protein, gene, gronemeyer, heterodimer, response, cells, dev, dna,
Topics {✒️}
peroxisome proliferator-activated receptor/retinoid peroxisome proliferator-activated receptor-retinoid intact vdr-rxr complex peroxisome proliferator-activated receptor peroxisome proliferator-activated receptors rxr[beta] ligand-binding domains unraveling protein-protein interactions month download article/chapter pml-rara/rxr alters ppar-rxr heterodimer activates human car/rxralpha heterodimer ra-induced rar[gamma] degradation specific sequence requirements retinoic acid-induced degradation farnesoid x-activated receptor rxr ligand-binding domains gampe rt jr receptor gamma-deficient mice dna binding specificity nuclear receptors sxr/pxr ligand-independent nuclear receptors small-cell lung cancer receptor α mediated prolactin gene transcription ligand-bound crystal structure retinoic acid receptor/retinoid fluorescence imaging reveals gene-specific permissivity ppar target genes ubiquitin-proteasome pathway multiple parameters control dr3 target dna vdr/rxr cistrome receptor heterodimer binding privacy choices/manage cookies specific dna requires multiple physiological processes ligand binding domain device instant download key cellular functions dna-induced dissociation human thyroid carcinomas forkhead protein foxa1 editor information editors analog bind rxralpha cognate response elements bifunctional enzyme gene human hepatocellular carcinoma receptor-gamma gene decreased dna binding
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ScholarlyArticle:
headline:RXRs: Collegial Partners
pageEnd:102
pageStart:75
image:https://media.springernature.com/w153/springer-static/cover/book/978-94-017-9050-5.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:The Biochemistry of Retinoic Acid Receptors I: Structure, Activation, and Function at the Molecular Level
isbn:
978-94-017-9050-5
978-94-017-9049-9
type:Book
publisher:
name:Springer Netherlands
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:Federica Gilardi
affiliation:
name:University of Lausanne
address:
name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
type:PostalAddress
type:Organization
type:Person
name:Béatrice Desvergne
affiliation:
name:University of Lausanne
address:
name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
type:PostalAddress
type:Organization
email:[email protected]
type:Person
keywords:Nuclear Receptor, Constitutive Androstane Receptor, Heterodimerization Partner, Nuclear Receptor Binding, Chicken Ovalbumin Upstream Promoter Transcription
description:Retinoid X Receptors (RXR) were initially identified as nuclear receptors binding with stereo-selectivity the vitamin A derivative 9-cis retinoic acid, although the relevance of this molecule as endogenous activator of RXRs is still elusive. Importantly, within the nuclear receptor superfamily, RXRs occupy a peculiar place, as they are obligatory partners for a number of other nuclear receptors, thus integrating the corresponding signaling pathways. In this chapter, we describe the structural features allowing RXR to form homo- and heterodimers, and the functional consequences of this unique ability. Furthermore, we discuss the importance of studying RXR activity at a genome-wide level in order to comprehensively address the biological implications of their action that is fundamental to understand to what extent RXRs could be exploited as new therapeutic targets.
datePublished:2014
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name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
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