Article
Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein.
Molecular endocrinology (Baltimore, Md.) - 1 Nov 1996
Weis K E, Ekena K, Thomas J A, Lazennec G, Katzenellenbogen B S
Abstract excerpt
To better understand structure-activity relationships in the human estrogen receptor (ER), we examined the role of tyrosine 537 in the transcriptional response of the receptor, since this residue is close to a region of the hormone-binding domain shown previously to be important in hormone-dependent transcriptional activity and because this amino acid has been proposed to be a tyrosine kinase phosphorylation site...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.