[HTML][HTML] Characterization of the Amino-terminal Activation Domain of Peroxisome Proliferator-activated Receptor α: IMPORTANCE OF α-HELICAL STRUCTURE IN …
R Hi, S Osada, N Yumoto, T Osumi - Journal of Biological Chemistry, 1999 - ASBMB
The transactivating function of the A/B region of mouse peroxisome proliferator-activated
receptor α (PPARα; NR1C1) was characterized. The truncated version of PPARα lacking the
A/B region had 60–70% lower transactivating function than full-length PPARα in both the
presence and absence of the peroxisome proliferator ciprofibrate. When tethered to the
yeast Gal4 DNA-binding domain, the A/B region exhibited the significant ligand-independent
transactivating function, AF-1 activity. The first 44 amino acid residues were necessary for …
receptor α (PPARα; NR1C1) was characterized. The truncated version of PPARα lacking the
A/B region had 60–70% lower transactivating function than full-length PPARα in both the
presence and absence of the peroxisome proliferator ciprofibrate. When tethered to the
yeast Gal4 DNA-binding domain, the A/B region exhibited the significant ligand-independent
transactivating function, AF-1 activity. The first 44 amino acid residues were necessary for …