John T. Moore

TL;DR: The identification of a human (h) orphan nuclear receptor, termed the pregnane X receptor (PXR), that binds to a response element in the CYP3A4 promoter and is activated by a range of drugs known to induce CYP 3A4 expression is reported.

TL;DR: The results provide evidence for the existence of a novel steroid hormone signaling pathway with potential implications in the regulation of steroid hormone and sterol homeostasis and the expression of the CYP3A family of steroid hydroxylases and modulates sterol and bile acid biosynthesis in vivo.

TL;DR: The crystal structure of the human GR ligand binding domain (LBD) bound to dexamethasone and a coactivator motif derived from the transcriptional intermediary factor 2 is reported to establish a framework for understanding the roles of protein-hormone and protein-protein interactions in GR signaling pathways.

TL;DR: Characterization of the three full length isoforms, hERβ1-3, by in vitro band shift studies indicated that the isoforms were able to form DNA-binding homodimers and heterodimer with each other and with the ERα subtype.

TL;DR: In this paper, the mouse and human pregnane X receptor (PXR) were shown to be activated by compounds that induce CYP3A expression in primary hepatocytes, and the authors reported the cloning and characterization of PXR from these two species, with the rabbit, rat and human receptors sharing only approximately 80% amino acid identity in their ligand-binding domains.