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

Allosteric Pathways in the PPARγ-RXRα nuclear receptor complex

29 Jan 2016

Abstract excerpt

Understanding the nature of allostery in DNA-nuclear receptor (NR) complexes is of fundamental importance for drug development since NRs regulate the transcription of a myriad of genes in humans and other metazoans. Here, we investigate allostery in the peroxisome proliferator-activated/retinoid X receptor heterodimer. This important NR complex is a target for antidiabetic drugs since it binds to DNA and...

Read the complete abstract on PubMed

Topics

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

Share to Adipose Tissue and Metabolism
Share to Peroxisome Proliferator-Activated Receptors
Share to Receptor Mechanisms and Signaling

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 26823026
DOI: 10.1038/srep19940

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric Pathways in the PPARγ-RXRα nuclear receptor complexPMID 26823026Read ↗

Structural and energetic differences between the human RXRα–PPARγ heterodimer with and without DNA bindingSemantic proximity Read ↗

Structural determinants of allosteric ligand activation in RXR heterodimers.Semantic proximity Read ↗

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation.Semantic proximity Read ↗

A molecular switch regulating transcriptional repression and activation of PPARγ.Semantic proximity Read ↗

Minireview: Dynamic Structures of Nuclear Hormone Receptors: New Promises and ChallengesSemantic proximity Read ↗

Conformational Changes of RORγ During Response Element Recognition and Coregulator EngagementSemantic proximity Read ↗

Single-Nucleotide Polymorphism of PPARγ, a Protein at the Crossroads of Physiological and Pathological Processes.Semantic proximity Read ↗

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

Interplay of protein disorder in retinoic acid receptor heterodimer and its corepressor regulates gene expressionSemantic proximity Read ↗

A Structural Signature Motif Enlightens the Origin and Diversification of Nuclear ReceptorsSemantic proximity Read ↗

Genetic variations within the ERE motif modulate plasticity and energetics of binding of DNA to the ERα nuclear receptor.Semantic proximity Read ↗

Helix 1/8 interactions influence the activity of nuclear receptor ligand-binding domains.Semantic proximity Read ↗

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