14667966

Source:http://linkedlifedata.com/resource/pubmed/id/14667966

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0034833, umls-concept:C0037083, umls-concept:C0040649, umls-concept:C0441712, umls-concept:C1710082
pubmed:issue	10-13
pubmed:dateCreated	2003-12-11
pubmed:abstractText	The diverse effects of progesterone on female reproductive tissues are mediated by the progesterone receptor (PR), a member of the nuclear receptor family of ligand-dependent transcription factors. Thus, PR is an important therapeutic target in female reproduction and in certain endocrine dependent cancers. This paper reviews our understanding of the mechanism of action of the most widely used PR antagonist RU486. Although RU486 is a competitive steroidal antagonist that can displace the natural hormone for PR, it's potency derives from additional "active antagonism" that involves inhibiting the activity of PR hormone agonist complexes in trans through heterodimerization and competition for binding to progesterone response elements on target DNA, and by recruitment of corepressors that have the potential to actively repress gene transcription. An additional functional role for PR has recently been defined whereby a subpopulation of PR in the cytoplasm or cell membrane is capable of mediating rapid progesterone induced activation of certain signal transduction pathways in the absence of gene transcription. This paper also reviews recent results on the mechanism of the extra-nuclear action of PR and the potential biological roles and implications of this novel PR signaling pathway.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/DK49030
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0404536
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Hormone Antagonists, http://linkedlifedata.com/resource/pubmed/chemical/Mifepristone, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Progesterone
pubmed:status	MEDLINE
pubmed:month	Nov
pubmed:issn	0039-128X
pubmed:author	pubmed-author:BoonyaratanakornkitVirojV, pubmed-author:EdwardsDean PDP, pubmed-author:LeonhardtSusan ASA
pubmed:issnType	Print
pubmed:volume	68
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	761-70
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:14667966-Animals, pubmed-meshheading:14667966-Cell Membrane, pubmed-meshheading:14667966-Cytoplasm, pubmed-meshheading:14667966-Dimerization, pubmed-meshheading:14667966-Female, pubmed-meshheading:14667966-Hormone Antagonists, pubmed-meshheading:14667966-Humans, pubmed-meshheading:14667966-Mifepristone, pubmed-meshheading:14667966-Models, Biological, pubmed-meshheading:14667966-Protein Binding, pubmed-meshheading:14667966-Protein Conformation, pubmed-meshheading:14667966-Protein Structure, Tertiary, pubmed-meshheading:14667966-Protein-Tyrosine Kinases, pubmed-meshheading:14667966-Receptors, Progesterone, pubmed-meshheading:14667966-Signal Transduction, pubmed-meshheading:14667966-Transcription, Genetic, pubmed-meshheading:14667966-Transcriptional Activation, pubmed-meshheading:14667966-src Homology Domains
pubmed:year	2003
pubmed:articleTitle	Progesterone receptor transcription and non-transcription signaling mechanisms.
pubmed:affiliation	Department of Pathology B216, School of Medicine University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Campus Box B216, Denver, CO 80262, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't