dc.creatorPresman, Diego Martin
dc.creatorHager, Gordon L.
dc.date.accessioned2018-11-21T18:22:10Z
dc.date.accessioned2022-10-15T12:31:47Z
dc.date.available2018-11-21T18:22:10Z
dc.date.available2022-10-15T12:31:47Z
dc.date.created2018-11-21T18:22:10Z
dc.date.issued2017-01-08
dc.identifierPresman, Diego Martin; Hager, Gordon L.; More than meets the dimer: What is the quaternary structure of the glucocorticoid receptor?; Taylor ; Transcription; 8; 1; 8-1-2017; 32-39
dc.identifier2154-1272
dc.identifierhttp://hdl.handle.net/11336/64876
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4386305
dc.description.abstractIt is widely accepted that the glucocorticoid receptor (GR), a ligand-regulated transcription factor that triggers anti-inflammatory responses, binds specific response elements as a homodimer. Here, we will discuss the original primary data that established this model and contrast it with a recent report characterizing the GR–DNA complex as a tetramer.
dc.languageeng
dc.publisherTaylor
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.tandfonline.com/doi/full/10.1080/21541264.2016.1249045
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1080/21541264.2016.1249045
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectDIMER
dc.subjectDNA BINDING
dc.subjectGLUCOCORTICOID RECEPTOR
dc.subjectMONOMER
dc.subjectSTEROID RECEPTORS
dc.subjectTETRAMER
dc.titleMore than meets the dimer: What is the quaternary structure of the glucocorticoid receptor?
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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