Evidence map›Paper›PMID 7479078›Full record

ArticleNucleic acids research1995

COUP-TF II homodimers are formed in preference to heterodimers with RXR alpha or TR beta in intact cells.

A J Butler, M G Parker

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

19 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
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  8. Choose your destiny: Make a cell fate decision with COUP-TFII.The Journal of steroid biochemistry and molecular biology · 2016
    Review
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  18. A role for Sp and nuclear receptor transcription factors in a cardiac hypertrophic growth program.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  19. Article
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.

A J ButlerLaboratory of Molecular Endocrinology, Imperial Cancer Research Fund, London, UK.
M G Parker
The Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chicken ovalbumin upstream promoter-transcription factor (COUP-TF) represses the transcriptional activity of a number of nuclear receptors, including that of retinoid receptors (RAR and RXR) and thyroid hormone receptors (TR). Since COUP-TF is capable of binding to DNA in vitro either as a homodimer or as a heterodimer with RXR or TR, it has not been possible to distinguish between competitive DNA binding and heterodimer formation as a mechanism to account for the repression. Using a two-hybrid system we have investigated the dimerisation properties of COUP-TF II in intact cells. In conditions where COUP-TF II homodimers and RXR alpha-RAR alpha heterodimers were formed we were unable to detect the formation of heterodimers between COUP-TF II and RXR alpha. Moreover, we were unable to detect an interaction between COUP-TF II and RXR alpha on DNA. Similarly COUP-TF II homodimers and RXR alpha-TR beta heterodimers are favoured over COUP-TF II-TR beta heterodimers. We conclude that the formation of functionally inactive heterodimers is unlikely to represent a general mechanism by which COUP-TF represses the transcriptional activity of nuclear receptors and favour a model in which repression is mediated by COUP-TF homodimers competing for binding to DNA.

Indexed as

DNA-Binding ProteinsReceptors, SteroidSaccharomyces cerevisiae ProteinsAnimalsBase SequenceBinding, CompetitiveCells, CulturedChick EmbryoCOUP Transcription FactorsDNAFibroblastsFungal ProteinsHumansModels, GeneticMolecular Sequence DataProtein ConformationCOUP Transcription FactorsDNADNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeReceptors, Retinoic AcidReceptors, SteroidReceptors, Thyroid HormoneRecombinant Fusion ProteinsRepressor ProteinsRetinoid X ReceptorsSaccharomyces cerevisiae ProteinsTranscription FactorsTretinoin

Identifiers

PMID7479078
PMCPMC307356
OpenAlexW2005754854

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.