ArticleEMBO reports2004
Signature of the oligomeric behaviour of nuclear receptors at the sequence and structural level.
Article in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.
- Pooled it
- The role of HNF4α in adenocarcinoma.Biochemical Society transactions · 2026Review
- Updated knowledge and a proposed nomenclature for nuclear receptors with two DNA binding domains (2DBD-NRs).PloS one · 2023Article
- Nuclear hormone receptor NHR-49 is an essential regulator of stress resilience and healthy aging inFrontiers in physiology · 2023Review
- Structural insights into the HNF4 biology.Frontiers in endocrinology · 2023Review
- Article
- A structural signature motif enlightens the origin and diversification of nuclear receptors.PLoS genetics · 2021Article
- Mediator subunit MDT-15/MED15 and Nuclear Receptor HIZR-1/HNF4 cooperate to regulate toxic metal stress responses in Caenorhabditis elegans.PLoS genetics · 2019Article
- A revisited version of the apo structure of the ligand-binding domain of the human nuclear receptor retinoic X receptor α.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Bioinformatic analysis of a novel Echinococcus granulosus nuclear receptor with two DNA binding domains.PloS one · 2019Article
- Novel Insights into the Pathogenesis of Monogenic Congenital Anomalies of the Kidney and Urinary Tract.Journal of the American Society of Nephrology : JASN · 2018Review
- Heterodimers of photoreceptor-specific nuclear receptor (PNR/NR2E3) and peroxisome proliferator-activated receptor-γ (PPARγ) are disrupted by retinal disease-associated mutations.Cell death & disease · 2017Article
- Article
- Gain-of-Function Alleles in Caenorhabditis elegans Nuclear Hormone Receptor nhr-49 Are Functionally Distinct.PloS one · 2016Article
- Predicting the relative binding affinity of mineralocorticoid receptor antagonists by density functional methods.Journal of computer-aided molecular design · 2015Article
- Structural basis of natural promoter recognition by the retinoid X nuclear receptor.Scientific reports · 2015Article
- Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics.PLoS computational biology · 2013Article
- Small-molecule hormones: molecular mechanisms of action.International journal of endocrinology · 2013Article
- Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Src tyrosine kinase phosphorylation of nuclear receptor HNF4α correlates with isoform-specific loss of HNF4α in human colon cancer.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear receptors (NRs) are ligand-dependent transcription factors that control a large number of physiological events through the regulation of gene transcription. NRs function either as homodimers or as heterodimers with retinoid X receptor/ultraspiracle protein (RXR/USP). A structure-based sequence analysis aimed at discovering the molecular mechanism that controls the dimeric association of the ligand-binding domain reveals two sets of differentially conserved residues, which partition the entire NR superfamily into two classes related to their oligomeric behaviour. Site-directed mutagenesis confirms the functional importance of these residues for the dimerization process and/or transcriptional activity. All homodimers belong to class I, in which the related residues contribute a communication pathway of two salt bridges linking helix 1 on the cofactor-binding site to the dimer interface. A salt bridge involving a differentially conserved arginine residue in loop H8-H9 defines the signature motif of heterodimers. RXR/USP and all Caenorhabditis elegans NRs belong to class I, supporting the hypothesis of an earlier emergence of this class.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.