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

Structural determinants of allosteric ligand activation in RXR heterodimers.

Cell - 6 Feb 2004

Shulman Andrew I, Larson Christopher, Mangelsdorf David J, Ranganathan Rama

Abstract excerpt

Allosteric communication underlies ligand-dependent transcriptional responses mediated by nuclear receptors. While studies have elucidated many of the components involved in this process, the energetic architecture within the receptor protein that mediates allostery remains unknown. Using a sequence-based method designed to detect coevolution of amino acids in a protein, termed the statistical coupling analysis...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Data Interpretation, Statistical
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ligands

Share to Receptors, Cytoplasmic and Nuclear

Share to Receptors, Retinoic Acid

Share to Retinoid X Receptors

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 15016376
DOI: 10.1016/s0092-8674(04)00119-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural determinants of allosteric ligand activation in RXR heterodimers.PMID 15016376Read ↗

Functional plasticity and evolutionary adaptation of allosteric regulation.Semantic proximity Read ↗

Rewiring Ancient Residue Interaction Networks Drove the Evolution of Specificity in Steroid Receptors.Semantic proximity Read ↗

Allosteric Pathways in the PPARγ-RXRα nuclear receptor complexSemantic proximity Read ↗

Evolutionary identification of a subtype specific functional site in the ligand binding domain of steroid receptors.Semantic proximity Read ↗

Allostery and coupled sequence variation in nuclear hormone receptors.Semantic proximity Read ↗

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

Evolutionary action and structural basis of the allosteric switch controlling β2AR functional selectivity.Semantic proximity Read ↗

Dimerization of G-protein-coupled receptors.Semantic proximity Read ↗

Vestigialization of an allosteric switch: genetic and structural mechanisms for the evolution of constitutive activity in a steroid hormone receptor.Semantic proximity Read ↗

Unique Features of Different Classes of G-Protein-Coupled Receptors Revealed from Sequence Coevolutionary and Structural AnalysisSemantic proximity Read ↗

Unique Features of Different Classes of G-Protein-Coupled Receptors Revealed from Sequence Coevolutionary and Structural AnalysisSemantic proximity Read ↗

Conservation and divergence in the allosteric architectures of five human protein kinasesSemantic proximity Read ↗

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