• Publications
  • Influence
Structural organization of mouse peroxisome proliferator-activated receptor gamma (mPPAR gamma) gene: alternative promoter use and different splicing yield two mPPAR gamma isoforms.
  • Y. Zhu, C. Qi, +4 authors J. Reddy
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 15 August 1995
The results establish that at least one of the PPAR genes yields more than one protein product, similar to that encountered with retinoid X receptor and retinoic acid receptor genes. Expand
Isolation and Characterization of PBP, a Protein That Interacts with Peroxisome Proliferator-activated Receptor*
PBP modestly increased the transcriptional activity of PPARγ, and a truncated form of PBP acted as a dominant-negative repressor, suggesting that PBP is a genuine coactivator for PPAR. Expand
Defect in Peroxisome Proliferator-activated Receptor α-inducible Fatty Acid Oxidation Determines the Severity of Hepatic Steatosis in Response to Fasting*
Observations point to the critical importance of PPARα in the transcriptional regulatory responses to fasting and in determining the severity of hepatic steatosis. Expand
Deletion of PBP/PPARBP, the Gene for Nuclear Receptor Coactivator Peroxisome Proliferator-activated Receptor-binding Protein, Results in Embryonic Lethality*
Observations suggest that there is no functional redundancy between PBP and other coactivators such as steroid receptor coactivator-1 and that PBP plays a critical role in the signaling of PPARγ and other nuclear receptors. Expand
Peroxisomal and Mitochondrial Fatty Acid β-Oxidation in Mice Nullizygous for Both Peroxisome Proliferator-activated Receptor α and Peroxisomal Fatty Acyl-CoA Oxidase
A critical role is defined for both PPARα and AOX in hepatic lipid metabolism and in the pathogenesis of specific fatty liver phenotype in livers with defective peroxisomal β-oxidation. Expand
Peroxisome proliferator-activated receptors, coactivators, and downstream targets
A multifaceted approach, which includes the identification of additional coactivators that may be responsible for cell specific transcriptional activation of PPAR-mediated target genes, and generation of genetically modified animals will be necessary to gain more insight into the upstream and downstream targets responsible for the induction of early and delayed PP-induced pleiotropic responses. Expand
Isolation and Characterization of Peroxisome Proliferator-activated Receptor (PPAR) Interacting Protein (PRIP) as a Coactivator for PPAR*
A truncated form of PRIP (peroxisome proliferator-activated receptorinteracting protein) acts as a dominant-negative repressor, suggesting that PRIP is a genuine coactivator. Expand
Defects of the Heart, Eye, and Megakaryocytes in Peroxisome Proliferator Activator Receptor-binding Protein (PBP) Null Embryos Implicate GATA Family of Transcription Factors*
It is shown that PBP is critical for the development of placenta and for the normal embryonic development of the heart, eye, vascular, and hematopoietic systems and the GATA family of transcription factors are identified as a new interacting partner of PBP. Expand
Cloning and characterization of PIMT, a protein with a methyltransferase domain, which interacts with and enhances nuclear receptor coactivator PRIP function
PIMT enhances the transcriptional activity of peroxisome proliferator-activated receptor γ and retinoid-X-receptor α, which is further stimulated by coexpression of PRIP, implying that PIMT is a component of nuclear receptor signal transduction apparatus acting through PRIP. Expand
Cloning and identification of mouse steroid receptor coactivator-1 (mSRC-1), as a coactivator of peroxisome proliferator-activated receptor gamma.
The isolated mouse steroid receptor coactivator (mSRC-1) involved in nuclear hormone receptor transcriptional activity as a mPPARgamma interactive protein is isolated and it is suggested that mS RC-1 interacts with PPargamma and plays a role in the PPARGamma-mediated signaling pathway. Expand