1201908-17-9Relevant academic research and scientific papers
Improvement of water-solubility of biarylcarboxylic acid peroxisome proliferator-activated receptor (PPAR) δ-selective partial agonists by disruption of molecular planarity/symmetry
Kasuga, Jun-Ichi,Ishikawa, Minoru,Yonehara, Mitsuhiro,Makishima, Makoto,Hashimoto, Yuichi,Miyachi, Hiroyuki
experimental part, p. 7164 - 7173 (2010/11/16)
To elucidate the molecular basis of peroxisome proliferator-activated receptor (PPAR) δ partial agonism, X-ray crystal structures of complexes of the PPARδ ligand-binding site with partial agonists are required. Unfortunately, reported PPARδ partial agoni
Novel biphenylcarboxylic acid peroxisome proliferator-activated receptor (PPAR) δ selective antagonists
Kasuga, Jun-ichi,Ishida, Seiichi,Yamasaki, Daisuke,Makishima, Makoto,Doi, Takefumi,Hashimoto, Yuichi,Miyachi, Hiroyuki
scheme or table, p. 6595 - 6599 (2010/06/14)
We designed and synthesized novel PPARδ antagonists based on the crystal structure of the PPARδ full agonist TIPP-204 bound to the PPARδ ligand-binding domain, in combination with our nuclear receptor helix 12 folding modification hypothesis. Representati
