Evidence map›Paper›PMID 17525795›Full record

ReviewNuclear receptor signaling2007

Kinases and protein phosphorylation as regulators of steroid hormone action.

Nancy L Weigel, Nicole L Moore

Open access · hybridAbstract readReview
In one paragraph

Review in Nuclear receptor signaling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Post-translational modifications of the progesterone receptors.The Journal of steroid biochemistry and molecular biology · 2014
    Review
  15. Article
  16. Review
  17. Evidence for orphan nuclear receptor TR4 in the etiology of Cushing disease.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Article
  19. Review
  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.

Nancy L WeigelDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas, USA. nweigel@bcm.edu
Nicole L Moore
Baylor College of Medicine · US

Funding

REGULATION OF HUMAN STEROID RECEPTORS BY PHOSPHORYLATIONR01CA057539 · NCI · BAYLOR COLLEGE OF MEDICINE · PI WEIGEL, NANCY L. · 1993 to 2010
$4.0M
NCI NIH HHS R01 CA057539NCI NIH HHS R01 CA57539
6 · The paper itself

Abstract

Although the primary signal for the activation of steroid hormone receptors is binding of hormone, there is increasing evidence that the activities of cell signaling pathways and the phosphorylation status of these transcription factors and their coregulators determine the overall response to the hormone. In some cases, enhanced cell signaling is sufficient to cause activation of receptors in medium depleted of steroids. Steroid receptors are targets for multiple kinases. Many of the phosphorylation sites contain Ser/Thr-Pro motifs implicating proline-directed kinases such as the cyclin-dependent kinases and the mitogen-activated kinases (MAPK) in receptor phosphorylation. Although some sites are constitutively phosphorylated, others are phosphorylated in response to hormone. Still others are only phosphorylated in response to specific cell signaling pathways. Phosphorylation of specific sites has been implicated not only in overall transcriptional activity, but also in nuclear localization, protein stability, and DNA binding. The studies of the roles of phosphorylation in coregulator function are more limited, but it is now well established that many of them are highly phosphorylated and that phosphorylation regulates their function. There is good evidence that some of the phosphorylation sites in the receptors and coregulators are targets of multiple signaling pathways. Individual sites have been associated both with functions that enhance the activity of the receptor, as well as with functions that inhibit activity. Thus, the specific combinations of phosphorylations of the steroid receptor combined with the expression levels and phosphorylation status of coregulators will determine the genes regulated and the biological response.

Indexed as

Models, BiologicalCell NucleusFeedbackGonadal Steroid HormonesNuclear ProteinsPhosphorylationPhosphotransferasesReceptors, Cytoplasmic and NuclearSignal TransductionGonadal Steroid HormonesNuclear ProteinsPhosphotransferasesReceptors, Cytoplasmic and Nuclear

Identifiers

PMID17525795
PMCPMC1876600
OpenAlexW1987431548

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.