Evidence map›Paper›PMID 10051577›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Thyroid hormone receptor-associated proteins and general positive cofactors mediate thyroid hormone receptor function in the absence of the TATA box-binding protein-associated factors of TFIID.

J D Fondell, M Guermah, S Malik, R G Roeder

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
13.6field-weighted citation impact, top 1% 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

50 citing papers in PubMed, 166 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Regulation of cardiac transcription by thyroid hormone and Med13.Journal of molecular and cellular cardiology · 2019
    Article
  7. Mutations in TBL1X Are Associated With Central Hypothyroidism.The Journal of clinical endocrinology and metabolism · 2016
    Observational
  8. Article
  9. Review
  10. Article
  11. General molecular biology and architecture of nuclear receptors.Current topics in medicinal chemistry · 2012
    Review
  12. Origins and activity of the Mediator complex.Seminars in cell & developmental biology · 2011
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Quantitative proteomic analysis of distinct mammalian Mediator complexes using normalized spectral abundance factors.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  20. 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

4 authors at 1 institution in 1 country.

J D FondellLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
M Guermah
S Malik
R G Roeder
Rockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coactivators previously implicated in ligand-dependent activation functions by thyroid hormone receptor (TR) include p300 and CREB-binding protein (CBP), the steroid receptor coactivator-1 (SRC-1)-related family of proteins, and the multicomponent TR-associated protein (TRAP) complex. Here we show that two positive cofactors (PC2 and PC4) derived from the upstream stimulatory activity (USA) cofactor fraction act synergistically to mediate thyroid hormone (T3)-dependent activation either by TR or by a TR-TRAP complex in an in vitro system reconstituted with purified factors and DNA templates. Significantly, the TRAP-mediated enhancement of activation by TR does not require the TATA box-binding protein-associated factors of TFIID. Furthermore, neither the pleiotropic coactivators CBP and p300 nor members of the SRC-1 family were detected in either the TR-TRAP complex or the other components of the in vitro assay system. These results show that activation by TR at the level of naked DNA templates is enhanced by cooperative functions of the TRAP coactivators and the general coactivators PC2 and PC4, and they further indicate a potential functional redundancy between TRAPs and TATA box-binding protein-associated factors in TFIID. In conjunction with earlier studies on other nuclear receptor-interacting cofactors, the present study also suggests a multistep pathway, involving distinct sets of cofactors, for activation of hormone responsive genes.

Indexed as

Transcription, GeneticAnimalsCarrier ProteinsCell LineDNA-Binding ProteinsGene Expression RegulationHumansModels, ChemicalProprotein Convertase 2Proprotein ConvertasesReceptors, Retinoic AcidReceptors, Thyroid HormoneRecombinant ProteinsRetinoid X ReceptorsSerine EndopeptidasesSpodopteraCarrier ProteinsDNA-Binding ProteinsPCSK4 protein, humanProprotein Convertase 2Proprotein ConvertasesReceptors, Retinoic AcidReceptors, Thyroid HormoneRecombinant ProteinsRetinoid X ReceptorsSerine EndopeptidasesSubtilisinsTATA-Box Binding ProteinTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIDTriiodothyronine

Identifiers

PMID10051577
PMCPMC26719
OpenAlexW2026291162

What OpenQuestion holds

Texttitle and abstract
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.