R
Ronald M. Evans
Researcher at Salk Institute for Biological Studies
Publications - 729
Citations - 176865
Ronald M. Evans is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Nuclear receptor & Receptor. The author has an hindex of 199, co-authored 708 publications receiving 166722 citations. Previous affiliations of Ronald M. Evans include Scripps Research Institute & University of California, Davis.
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Journal ArticleDOI
Humanized xenobiotic response in mice expressing nuclear receptor SXR.
Wen Xie,Joyce L. Barwick,Michael Downes,Bruce Blumberg,Cynthia M. Simon,Michael C. Nelson,Brent A. Neuschwander-Tetri,Elizabeth M. Brunt,Philip S. Guzelian,Ronald M. Evans +9 more
TL;DR: It is shown that targeted disruption of the mouse PXR gene abolishes induction of CYP3A by prototypic inducers such as dexamethasone or pregnenolone-16α-carbonitrile, and that SXR/PXR genes encode the primary species-specific xeno-sensors that mediate the adaptive hepatic response, and may represent the critical biochemical mechanism of human xenoprotection.
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A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR.
David J. Mangelsdorf,David J. Mangelsdorf,Kazuhiko Umesono,Kazuhiko Umesono,Steven A. Kliewer,Uwe Borgmeyer,Estelita S. Ong,Estelita S. Ong,Ronald M. Evans,Ronald M. Evans +9 more
TL;DR: Evidence is provided that expression of the gene for cellular retinol-binding protein type II (CRBPII), a key protein in the intestinal absorption of vitamin A, is dramatically up-regulated by retinoic acid in the presence of RXR but not RAR, suggesting that an RXR-mediated pathway exists for modulating vitamin A metabolism.
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RXR alpha mutant mice establish a genetic basis for vitamin A signaling in heart morphogenesis.
TL;DR: These results ascribe an essential function for the RXR alpha gene in embryonic development and provide the first evidence of a requirement for RXR in one of its predicted hormone response pathways.
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Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase.
Hongwu Chen,Richard J. Lin,Richard J. Lin,Wen Xie,Damien Wilpitz,Ronald M. Evans,Ronald M. Evans +6 more
TL;DR: In exploring the underlying mechanism, it is found that the acetylase ACTR can be acetylated by p300/CBP, and this results provide strong in vivo evidence that histone acetylation plays a key role in hormone-induced gene activation and defines cofactor acetylations as a novel regulatory mechanism in hormonal signaling.
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Unique response pathways are established by allosteric interactions among nuclear hormone receptors
TL;DR: It is suggested that allostery is a critical feature underlying the generation of diversity in hormone response networks through allosteric interactions among heterodimers create complexes with unique properties.