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Article

Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR.

Molecular and cellular endocrinology - 25 Jan 1999

Gorla-Bajszczak A, Juge-Aubry C, Pernin A, Burger A G, Meier C A

Abstract excerpt

The peroxisome proliferator-activated receptors (PPARs) are members of the nuclear hormone receptor superfamily. These ligand-activated transcription factors are implicated in the regulation of lipid metabolism and adipocyte differentiation and in the regulation of anti-inflammatory processes. In...

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PMID: 10195690
DOI: 10.1016/s0303-7207(98)00217-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-10195690-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

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Conserved amino acids in the ligand-binding and tau(i) domains of the peroxisome proliferator-activated receptor alpha are necessary for heterodimerization with RXR.PMID 10195690Read ↗

Alteration of a single amino acid in peroxisome proliferator-activated receptor-alpha (PPAR alpha) generates a PPAR delta phenotype.Semantic proximity Read ↗

Structural determinants of the agonist-independent association of human peroxisome proliferator-activated receptors with coactivators.Semantic proximity Read ↗

International Union of Pharmacology. LXI. Peroxisome proliferator-activated receptors.Semantic proximity Read ↗

Heterodimer formation with retinoic acid receptor RXRα modulates coactivator recruitment by peroxisome proliferator-activated receptor PPARγ.Semantic proximity Read ↗

Substitution of a conserved amino acid residue alters the ligand binding properties of peroxisome proliferator activated receptors.Semantic proximity Read ↗

Identification of critical residues for heterodimerization within the ligand-binding domain of retinoid X receptor.Semantic proximity Read ↗

Isolation and characterization of peroxisome proliferator-activated receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.Semantic proximity Read ↗

Three amino acids specify coactivator choice by retinoid X receptors.Semantic proximity Read ↗

A single amino acid change in the mouse peroxisome proliferator-activated receptor alpha alters transcriptional responses to peroxisome proliferators.Semantic proximity Read ↗

Tyrosine agonists reverse the molecular defects associated with dominant-negative mutations in human peroxisome proliferator-activated receptor gamma.Semantic proximity Read ↗

Structural basis of the transactivation deficiency of the human PPARγ F360L mutant associated with familial partial lipodystrophy.Semantic proximity Read ↗

Peroxisome proliferator-activated receptors and retinoic acid receptors differentially control the interactions of retinoid X receptor heterodimers with ligands, coactivators, and corepressors.Semantic proximity Read ↗

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