Evidence map›Paper›PMID 15650024›Full record

ArticleMolecular endocrinology (Baltimore, Md.)2005

Heterodimers of retinoic acid receptors and thyroid hormone receptors display unique combinatorial regulatory properties.

Sangho Lee, Martin L Privalsky

Open access · bronzeAbstract read
In one paragraph

Article in Molecular endocrinology (Baltimore, Md.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. The Influences of RARγ on the Behavior of Normal and Cancer Stem Cells.International journal of molecular sciences · 2026
    Review
  4. Rat embryonic stem cell-basedFrontiers in toxicology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Thyroid Hormone Mediated Modulation of Energy Expenditure.International journal of molecular sciences · 2015
    Review
  17. Article
  18. Article
  19. Krüppel-like factors are effectors of nuclear receptor signaling.General and comparative endocrinology · 2014
    Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Sangho LeeSection of Microbiology, One Shields Avenue, University of California at Davis, Davis, California 95616, USA.
Martin L Privalsky
University of California, Davis · US

Funding

MECHANISM OF ACTION OF THE VERB A ONCOGENE OF AEVR37CA053394 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1994 to 2012
$3.4M
Role of cofactors in nuclear hormone receptor function.R01DK053528 · NIDDK · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1998 to 2012
$2.9M
NCI NIH HHS R37 CA053394NCI NIH HHS R37 CA53394NIDDK NIH HHS R01 DK053528
6 · The paper itself

Abstract

Nuclear receptors are ligand-regulated transcription factors that regulate key aspects of metazoan development, differentiation, and homeostasis. Nuclear receptors recognize target genes by binding to specific DNA recognition sequences, denoted hormone response elements (HREs). Many nuclear receptors can recognize HREs as either homodimers or heterodimers. Retinoid X receptors (RXRs), in particular, serve as important heterodimer partners for many other nuclear receptors, including thyroid hormone receptors (TRs), and RXR/TR heterodimers have been proposed to be the primary mediators of target gene regulation by T3 hormone. Here, we report that the retinoic acid receptors (RARs), a distinct class of nuclear receptors, are also efficient heterodimer partners for TRs. These RAR/TR heterodimers form with similar affinities as RXR/TR heterodimers on an assortment of consensus and natural HREs, and preferentially assemble with the RAR partner 5' of the TR moiety. The corepressor and coactivator recruitment properties of these RAR/TR heterodimers and their transcriptional activities in vivo are distinct from those observed with the corresponding RXR heterodimers. Our studies indicate that RXRs are not unique in their ability to partner with TRs, and that RARs can also serve as robust heterodimer partners and combinatorial regulators of T3-modulated gene expression.

Indexed as

Transcriptional ActivationAnimalsDimerizationDNA-Binding ProteinsGenes, ReporterHistone AcetyltransferasesHumansNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 3Receptors, Retinoic AcidResponse ElementsRetinoic Acid Receptor alphaRetinoid X Receptor gammaThyroid Hormone Receptors alphaTranscription FactorsTriiodothyronineDNA-Binding ProteinsHistone AcetyltransferasesNCOA1 protein, humanNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 3RARA protein, humanReceptors, Retinoic AcidRetinoic Acid Receptor alphaRetinoid X Receptor gammaThyroid Hormone Receptors alphaTranscription FactorsTriiodothyronine

Identifiers

PMID15650024
PMCPMC2675561
OpenAlexW2146073537

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.