Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARα

By H. Eric Xu, Thomas B. Stanley, V. Montana, M. Lambert, B. Shearer, J. Cobb, D. D. Mckee, C. Galardi, K. D. Plunket, Robert T. Nolte and 5 more. Nature, 2002

630 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/9b97373986f051f43eda9ef9c2feff1ca6e75d03

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. S. Kersten
2. Mitchell A. Lazar
3. Bart Staels
4. Manabu T. Nakamura
5. J. Loor
6. M. Lehrke
7. D. Cohen
8. Y. Kawano

Citations in the corpus

• Regulation of energy metabolism by long-chain fatty acids. (2014, background): “On the other hand, a synthetic antagonist blocks AF2 taking an active position, allowing a corepressor to stay bound [35].”
• The many faces of PPARgamma. (2005, positive): “In addition, as the corepressors and coactivators interface with overlapping surfaces on the receptor (Hu and Lazar, 1999; Xu et al., 2002), partial agonism may also result from ligand inducing an intermediate conformation that is recognized by both classes of cofactors.”
• Overview of Nomenclature of Nuclear Receptors (2006, background): “In contrast with other antagonist-bound NR structures, the AF-2 helix 12 undergoes a rigid body shift toward the N terminus of helix 3 and is loosely packed against this helix, leaving sufficient space to accommodate the corepressor motif (Xu et al., 2002).”
• Peroxisome Proliferator-Activated Receptor Alpha Target Genes (2010, background): “Activation of transcription by PPARs is dependent on a number of different steps including ligand binding to PPAR, binding of PPAR to the target gene, removal of corepressors and recruitment of coactivators, remodeling of the chromatin structure, and finally facilitation of gene transcription [7].”