D
Dean P. Edwards
Researcher at Baylor College of Medicine
Publications - 229
Citations - 14837
Dean P. Edwards is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: Progesterone receptor & Receptor. The author has an hindex of 71, co-authored 226 publications receiving 13938 citations. Previous affiliations of Dean P. Edwards include University of Illinois at Urbana–Champaign & North Carolina State University.
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Journal ArticleDOI
Progesterone receptor contains a proline-rich motif that directly interacts with SH3 domains and activates c-Src family tyrosine kinases.
Viroj Boonyaratanakornkit,Margaret Porter Scott,Vered Ribon,Vered Ribon,Lori Sherman,Steven M. Anderson,James L. Maller,W. Todd Miller,Dean P. Edwards +8 more
TL;DR: It is shown that rapid progestin-induced activation of Src and downstream MAP kinase in mammalian cells is dependent on PR-SH3 domain interaction, but not on the transcriptional activity of PR.
Journal ArticleDOI
Progesterone Receptor Isoform A But Not B Is Expressed in Endometriosis
TL;DR: It is concluded that progesterone resistance in endometriotic tissue from laboratory and clinical observations may be accounted for by the presence of the inhibitory PR isoform PR-A and the absence of the stimulatory isoforms PR-B.
Journal ArticleDOI
Regulation of signal transduction pathways by estrogen and progesterone
TL;DR: The nature of the receptors that mediate rapid signaling actions of estrogen and progesterone are reviewed, the signaling molecules and pathways involved, the mechanisms by which receptors couple with components of signaling complexes and trigger responses, and the target tissues and cell functions regulated by this mode of steroid hormone action are described.
Journal ArticleDOI
The Steroid Receptor Coactivator-1 Contains Multiple Receptor Interacting and Activation Domains That Cooperatively Enhance the Activation Function 1 (AF1) and AF2 Domains of Steroid Receptors
Sergio A. Onate,Viroj Boonyaratanakornkit,Thomas E. Spencer,Sophia Y. Tsai,Ming-Jer Tsai,Dean P. Edwards,Bert W. O'Malley +6 more
TL;DR: It is shown that SRC-1 is a modular coactivator that possesses intrinsic transcriptional activity when tethered to DNA and that it harbors two distinct activation domains, AD1 and AD2, needed for the maximum coactivation function of steroid receptors.
Journal ArticleDOI
The opposing transcriptional activities of the two isoforms of the human progesterone receptor are due to differential cofactor binding.
TL;DR: It is proposed that hPRA is transcriptionally inactive due to its inability to efficiently recruit coactivators, and the ability of PR to interact with cofactors in a productive manner is regulated by sequences contained within the amino terminus of the receptors.