Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor α and liver-X-receptor α
- 25 November 1998
- journal article
- Published by Elsevier in Molecular and Cellular Endocrinology
- Vol. 146 (1-2) , 69-76
- https://doi.org/10.1016/s0303-7207(98)00196-8
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- A Regulatory Role for RIP140 in Nuclear Receptor ActivationMolecular Endocrinology, 1998
- Subtype- and response element-dependent differences in transactivation by peroxisome proliferator-activated receptors α and γMolecular and Cellular Endocrinology, 1998
- PPARγ Promotes Monocyte/Macrophage Differentiation and Uptake of Oxidized LDLCell, 1998
- Oxidized LDL Regulates Macrophage Gene Expression through Ligand Activation of PPARγCell, 1998
- Ligand-induced Peroxisome Proliferator-activated Receptor α Conformational ChangeJournal of Biological Chemistry, 1997
- An oxysterol signalling pathway mediated by the nuclear receptor LXRαNature, 1996
- The peroxisome proliferator activated receptors (PPARs) and their effects on lipid metabolism and adipocyte differentiationBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1996
- A CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear ReceptorsCell, 1996
- The Orphan Nuclear Hormone Receptor LXRα Interacts with the Peroxisome Proliferator-activated Receptor and Inhibits Peroxisome Proliferator SignalingPublished by Elsevier ,1996
- Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressorNature, 1995