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<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd> <responseDate>2018-01-15T18:26:07Z</responseDate> <request identifier=oai:HAL:hal-01237073v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:hal-01237073v1</identifier> <datestamp>2017-12-21</datestamp> <setSpec>type:COUV</setSpec> <setSpec>subject:sdv</setSpec> <setSpec>collection:UNIV-RENNES1</setSpec> <setSpec>collection:UNIV-AG</setSpec> <setSpec>collection:IRSET</setSpec> <setSpec>collection:IRSET-TREC</setSpec> <setSpec>collection:IFR140</setSpec> <setSpec>collection:BIOSIT</setSpec> <setSpec>collection:INSERM</setSpec> <setSpec>collection:UR1-UFR-SVE</setSpec> <setSpec>collection:STATS-UR1</setSpec> <setSpec>collection:UR1-SDV</setSpec> <setSpec>collection:UR1-HAL</setSpec> <setSpec>collection:EHESP</setSpec> <setSpec>collection:USPC</setSpec> <setSpec>collection:IRSET-6</setSpec> <setSpec>collection:UNIV-ANGERS</setSpec> </header> <metadata><dc> <publisher>HAL CCSD</publisher> <title lang=en>The Synonymous Ala87 Mutation of Estrogen Receptor Alpha Modifies Transcriptional Activation Through Both ERE and AP1 Sites</title> <creator>Fernández-Calero, Tamara</creator> <creator>Flouriot, Gilles</creator> <creator>Marin, Mónica</creator> <contributor>Biochemistry-Molecular Biology ; Universidad de la Republica-Facultad de Medicina</contributor> <contributor>Bioinformatics Unit ; Institut Pasteur Montevideo</contributor> <contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor> <description>International audience</description> <identifier>ISBN : 978-1-4939-3126-2</identifier> <source>Estrogen Receptors</source> <contributor>Eyster, Kathleen M (ed)</contributor> <publisher>Springer New York</publisher> <identifier>hal-01237073</identifier> <identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01237073</identifier> <source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01237073</source> <source>Eyster, Kathleen M (ed). Estrogen Receptors, Springer New York, pp.287--296, 2016, Methods in Molecular Biology, 978-1-4939-3126-2. 〈10.1007/978-1-4939-3127-9_22〉</source> <identifier>DOI : 10.1007/978-1-4939-3127-9_22</identifier> <relation>info:eu-repo/semantics/altIdentifier/doi/10.1007/978-1-4939-3127-9_22</relation> <language>en</language> <subject lang=en>AP-1AP-1 pathwayAP-1 pathway</subject> <subject lang=en>EstrogenEstrogen receptorEstrogen receptor alanine 87 polymorphismEstrogen receptor alanine 87 polymorphism</subject> <subject lang=en>EstrogenEstrogen receptorEstrogen receptor alphaEstrogen receptor alpha (ERαERα )</subject> <subject lang=en>EstrogenEstrogen -responsive element (EREERE )</subject> <subject lang=en>EstrogenEstrogen transcriptional regulationEstrogen transcriptional regulation</subject> <subject lang=en>Nonclassical pathwayNonclassical pathway</subject> <subject>[SDV] Life Sciences [q-bio]</subject> <type>info:eu-repo/semantics/bookPart</type> <type>Book sections</type> <description lang=en>Estrogen receptor α (ERα) exerts regulatory actions through genomic mechanisms. In the classical pathway, ligand-activated ERα binds directly to DNA through estrogen response elements (ERE) located in the promoter of target genes. ERα can also exert indirect regulation of transcription via protein-protein interaction with other transcription factors such as AP-1. Several ERα synonymous polymorphisms have been identified and efforts to understand their implications have been made. Nevertheless effects of synonymous polymorphisms are still neglected. This chapter focuses on the experimental procedure employed in order to characterize the transcriptional activity of a synonymous polymorphism of the ERα (rs746432) called Alanine 87 (Ala87). Activity of both WT and Ala87 ERα isoforms on transcriptional pathways can be analyzed in transiently transfected cells using different reporter constructs. ERα efficiency on the classical genomic pathway can be analyzed by determining its transactivation activity on an ERE-driven thymidine kinase (TK) promoter controlling the expression of the luciferase reporter gene. Transcriptional activity through the indirect genomic pathway can be analyzed by employing an AP-1 DNA response element-driven promoter also controlling the expression of luciferase reporter gene</description> <date>2016</date> </dc> </metadata> </record> </GetRecord> </OAI-PMH>