Evidence map›Paper›PMID 9742089›Full record

ArticleMolecular and cellular biology1998

Transcriptional silencing is defined by isoform- and heterodimer-specific interactions between nuclear hormone receptors and corepressors.

C W Wong, M L Privalsky

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Rescue of a primary myelofibrosis model by retinoid-antagonist therapy.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Liganded RARalpha and RARgamma interact with but are repressed by TNIP1.Biochemical and biophysical research communications · 2009
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 1 institution in 1 country.

C W WongSection of Microbiology, Division of Biological Sciences, University of California at Davis, Davis, California 95616, USA.
M 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
MECHANISM OF ACTION OF THE V-ERB A ONCOGENE OF AEVR01CA053394 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI PRIVALSKY, MARTIN L. · 1991 to 1993
–
NCI NIH HHS CA53394NCI NIH HHS R37 CA053394
6 · The paper itself

Abstract

Nuclear hormone receptors are ligand-regulated transcription factors that play critical roles in metazoan homeostasis, development, and reproduction. Many nuclear hormone receptors exhibit bimodal transcriptional properties and can either repress or activate the expression of a given target gene. Repression appears to require a physical interaction between a receptor and a corepressor complex containing the SMRT/TRAC or N-CoR/RIP13 polypeptides. We wished to better elucidate the rules governing the association of receptors with corepressors. We report here that different receptors interact with different domains in the SMRT and N-CoR corepressors and that these divergent interactions may therefore contribute to distinct repression phenotypes. Intriguingly, different isoforms of a single nuclear hormone receptor class also differ markedly in their interactions with corepressors, indicative of their nonidentical actions in cellular regulation. Finally, we present evidence that combinatorial interactions between different receptors can, through the formation of heterodimeric receptors, result in novel receptor-corepressor interactions not observed for homomeric receptors.

Indexed as

Transcription, GeneticAmino Acid SequenceAnimalsBinding SitesCell LineCell NucleusChlorocebus aethiopsDimerizationDNA-Binding ProteinsHumansMolecular Sequence DataNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2Receptors, Cell SurfaceReceptors, Retinoic AcidDNA-Binding ProteinsNCOR1 protein, humanNCOR2 protein, humanNuclear ProteinsNuclear Receptor Co-Repressor 1Nuclear Receptor Co-Repressor 2RARA protein, humanReceptors, Cell SurfaceReceptors, Retinoic AcidRepressor ProteinsRetinoic Acid Receptor alpharetinoic acid receptor betaRetinoic Acid Receptor gamma

Identifiers

PMID9742089
PMCPMC109158
OpenAlexW2105048514

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.