Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Three amino acids specify coactivator choice by retinoid X receptors.

Molecular endocrinology (Baltimore, Md.) - 1 Aug 2000

Shao G, Heyman R A, Schulman I G

Abstract excerpt

Binding of agonists to nuclear receptors results in a conformational change in receptor structure that promotes interaction between activated receptors and coactivators. Receptor-coactivator interactions are mediated by the agonist-dependent formation of a hydrophobic pocket on the part of recept...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to CREB-Binding Protein
Share to Histone Acetyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Receptor Coactivator 1

Share to Receptors, Cytoplasmic and Nuclear

Share to Receptors, Retinoic Acid

Share to Retinoid X Receptors

Share to Trans-Activators

Source

Identifiers

PMID: 10935544
DOI: 10.1210/mend.14.8.0495

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Prepared record publication-10935544-2026-09-05.1. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Three amino acids specify coactivator choice by retinoid X receptors.PMID 10935544Read ↗

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

Nuclear receptor-coregulator interaction profiling identifies TRIP3 as a novel peroxisome proliferator-activated receptor gamma cofactor.Semantic proximity Read ↗

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

T0070907, a selective ligand for peroxisome proliferator-activated receptor gamma, functions as an antagonist of biochemical and cellular activities.Semantic proximity Read ↗

International Union of Pharmacology. LXIII. Retinoid X receptors.Semantic proximity Read ↗

Co-repressor release but not ligand binding is a prerequisite for transcription activation by human retinoid acid receptor alpha ligand-binding domain.Semantic proximity Read ↗

A dominant-negative peroxisome proliferator-activated receptor gamma (PPARgamma) mutant is a constitutive repressor and inhibits PPARgamma-mediated adipogenesis.Semantic proximity Read ↗

International Union of Pharmacology. LX. Retinoic acid receptors.Semantic proximity Read ↗

Evaluation of the Ligand-Dependent Coactivator Recruitment of the Nuclear Receptor Pregnane X Receptor Using Its Three-Alanine Residues-Inserted Mutant.Semantic proximity Read ↗

Both coactivator LXXLL motif-dependent and -independent interactions are required for peroxisome proliferator-activated receptor gamma (PPARgamma) function.Semantic proximity Read ↗

An Ideal PPAR Response Element Bound to and Activated by PPARα.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.