Professor
Department of Molecular Therapeutics
Florida Campus
tburris@scripps.edu
(561) 228-2217
Professor, Department of Metabolism & Aging
Faculty, Kellogg School of Science and Technology
Nuclear hormone receptors are ligand activated transcription factors that regulate a variety of physiological functions including development, metabolism, immune function, and reproduction. The best known members of this superfamily of receptors are the steroid receptors but also included in this group are receptors for fatty acids, bile acids, oxidized cholesterol, thyroid hormone, and lipophilic vitamins. Our group is focused on using chemical biology approaches to characterizing the physiological roles of these receptors as well as developing drugs targeting nuclear receptors for treatment of diseases including type 2 diabetes, heart disease, cancer and Alzheimer's disease. One particular area where we have concentrated over the past several years is identifying the ligands for a group of these receptors known as orphans. The “hormones” that bind to these orphan receptors have yet to be discovered.
B.A., Chemistry, Southern Illinois University
Ph.D., Molecular Biophysics, The Florida State University
Editorial Boards
Journal of Biological Chemistry
Endocrinology
Molecular Pharmacology
Burris TP. Nuclear Hormone Receptors for Heme: REV-ERBα and REV-ERBβ are Ligand Regulated Components of the Mammalian Clock. Molecular Endocrinolog 2008 22:1509-1520.
Wang Y, Rogers PM, Su C, Varga G, Burris TP Regulation of Cholesterologensis by the Oxysterol Receptor, LXRα. Journal of Biological Chemistry 2008 283:26332-26339.
Chandra V, Huang P, Raghuram S, Hamuro Y, Wang Y, Burris TP, Rastinejad F Structural Organization of the Intact PPARγ-RXRα Nuclear Receptor Complex on DNA. Nature 2008 456:350-356 (article). Comment in Cell Metabolism 2008, 9:8-10. (Faculty of 1000 "exceptional" paper).
Raghuram S, Stayrook KR, Huang P, Rogers PM, Noise AK, McClure DB, Burris LL, Khorasanizadeh S, Burris TP*, Rastinejad F* Identification of Heme as the Ligand for the Orphan Receptors REV-ERBα and REV-ERBβ. Nature Structural and Molecular Biology 2007 14:1207-1213. * Equal contributors and corresponding author. Research Highlights Nature Medicine 2007 13:1422; Leading Edge Cell 2007 131:1023; Research Highlights Nature Chemical Biology 2008 4:23. (Faculty of 1000 "must read" paper)