Article

A Structural Signature Motif Enlightens the Origin and Diversification of Nuclear Receptors

2020-11-20

Abstract excerpt

Nuclear receptors are ligand-activated transcription factors that modulate gene regulatory networks from embryonic development to adult physiology and thus represent major targets for clinical interventions in many diseases. Most nuclear receptors function either as homodimers or as heterodimers. The dimerization is crucial for gene regulation by nuclear receptors, by extending the repertoire of binding sites in t...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 956643ee-d530-53ce-a243-69aea719cbc0
DOI: 10.1101/2020.11.18.388405

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

A Structural Signature Motif Enlightens the Origin and Diversification of Nuclear ReceptorsDOI 10.1101/2020.11.18.388405Read

Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level.Semantic proximity Read

A comprehensive structural and functional analysis of the ligand binding domain of the nuclear receptor superfamily reveals highly conserved signaling motifs and two distinct canonical forms through evolutionSemantic proximity Read

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

Maturing of the nuclear receptor family.Semantic proximity Read

The multimerization pathway of the glucocorticoid receptorSemantic proximity Read

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

Nuclear Hormone Receptor Coregulators In Action: Diversity For Shared TasksSemantic proximity Read

Structural Insights Into Thyroid Hormone ReceptorsSemantic proximity Read

Structural insights into the HNF4 biologySemantic proximity Read

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

A family-based approach reveals the function of residues in the nuclear receptor ligand-binding domain.Semantic proximity Read

Mutation of two residues converts the ligand-binding domain of RXRα into a uniform monomer without impairing the binding of retinoic acid and cofactors.Semantic proximity Read