Isolation and characterization of a transcriptional cofactor and its novel isoform that bind the deoxyribonucleic acid-binding domain of peroxisome proliferator-activated receptor-gamma.

@article{Tomaru2006IsolationAC,
  title={Isolation and characterization of a transcriptional cofactor and its novel isoform that bind the deoxyribonucleic acid-binding domain of peroxisome proliferator-activated receptor-gamma.},
  author={Takuya Tomaru and Teturou Satoh and Satoshi Yoshino and Takahiro Ishizuka and Koshi Hashimoto and Tsuyoshi Monden and Masanobu Yamada and Masatomo Mori},
  journal={Endocrinology},
  year={2006},
  volume={147 1},
  pages={377-88}
}
Using the DNA-binding domain (DBD) and hinge region of human peroxisome proliferator-activated receptor (PPAR)-gamma as bait in yeast two-hybrid screen, we isolated partial cDNA identical with that of the C terminal of KIAA1769. KIAA1769 encodes a 2080-amino acid protein (molecular mass, 231 kDa) that was recently identified to interact with PPARalpha and termed PPARalpha-interacting cofactor 285 (here referred to as PPARgamma-DBD-interacting protein 1 (PDIP1)-alpha). PDIP1 mRNA was expressed… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

Coactivators in PPAR-Regulated Gene Expression

PPAR research • 2010
View 8 Excerpts
Highly Influenced

A rare nonsynonymous variant in the lipid metabolic gene HELZ2 related to primary biliary cirrhosis in Chinese Han.

Allergy, asthma, and clinical immunology : official journal of the Canadian Society of Allergy and Clinical Immunology • 2016
View 1 Excerpt

Similar Papers

Loading similar papers…