Journal article
The Orphan Nuclear Hormone Receptor LXRα Interacts with the Peroxisome Proliferator-activated Receptor and Inhibits Peroxisome Proliferator Signaling (∗)
Abstract
The yeast two-hybrid system was used to isolate novel cellular factors that interact with the mouse peroxisome proliferator-activated receptor alpha (PPARalpha). One of the interacting clones isolated encoded LXRalpha, a recently described human orphan nuclear hormone receptor. LXRalpha bound directly to PPARalpha, as well as to the common heterodimerization partner 9-cis-retinoic acid receptor (RXRalpha). LXRalpha did not form a DNA binding …
Authors
Miyata KS; McCaw SE; Patel HV; Rachubinski RA; Capone JP
Journal
Journal of Biological Chemistry, Vol. 271, No. 16, pp. 9189–9192
Publisher
Elsevier
Publication Date
4 1996
DOI
10.1074/jbc.271.16.9189
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
AnimalsBase SequenceBinding SitesCell LineCloning, MolecularConsensus SequenceDNA-Binding ProteinsHumansLiver X ReceptorsMacromolecular SubstancesMiceMicrobodiesMolecular Sequence DataOligodeoxyribonucleotidesOrphan Nuclear ReceptorsProtein BiosynthesisReceptors, Cytoplasmic and NuclearReceptors, Retinoic AcidRecombinant Fusion ProteinsRepetitive Sequences, Nucleic AcidRetinoid X ReceptorsSignal TransductionTranscription FactorsTranscription, GeneticTretinoin