Evidence map›Paper›PMID 24333793›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2014

Post-translational modifications of the progesterone receptors.

Hany A Abdel-Hafiz, Kathryn B Horwitz

Abstract readReview
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Article
  3. Hormone Signaling in Breast Development and Cancer.Advances in experimental medicine and biology · 2025
    Review
  4. Article
  5. Review
  6. The hormonal control of parturition.Physiological reviews · 2024
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. P38α MAPK is a gatekeeper of uterine progesterone responsiveness at peri-implantation via Ube3c-mediated PGR degradation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Endocrine disruptors of sex hormone activities.Molecular and cellular endocrinology · 2022
    Review
  15. Review
  16. Review
  17. Review
  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.

Hany A Abdel-HafizDivision of Endocrinology, Department of Medicine, Anschutz Medical Campus, University of Colorado Denver, Aurora, CO 80045, USA. Electronic address: hany.abdel-hafiz@ucdenver.edu.
Kathryn B HorwitzDivision of Endocrinology, Department of Medicine, Anschutz Medical Campus, University of Colorado Denver, Aurora, CO 80045, USA; Department of Pathology, Anschutz Medical Campus, University of Colorado Denver, Aurora, CO 80045, USA.
University of Colorado Denver · US

Funding

PROGESTERONE RECEPTORS IN BREAST CANCERR01CA026869 · NCI · UNIVERSITY OF COLORADO DENVER · PI HORWITZ, KATHRYN B · 1985 to 2014
$5.6M
NCI NIH HHS R01 CA026869NCI NIH HHS R01-CA026869-33
6 · The paper itself

Abstract

Progesterone plays a key role in the development, differentiation and maintenance of female reproductive tissues and has multiple non-reproductive neural functions. Depending on the cell and tissue, the hormonal environment, growth conditions and the developmental stage, progesterone can either stimulate cell growth or inhibit it while promoting differentiation. Progesterone receptors (PRs) belong to the steroid hormone receptor superfamily of ligand-dependent transcription factors. PR proteins are subject to extensive post-translational modifications that include phosphorylation, acetylation, ubiquitination and SUMOylation. The interplay among these modifications is complex with alteration of the receptors by one factor influencing the impact of another. Control over these modifications is species-, tissue- and cell-specific. They in turn regulate multiple functions including PR stability, their subcellular localization, protein-protein interactions and transcriptional activity. These complexities may explain how tissue- and gene-specific differences in regulation are achieved in the same organism, by the same receptor protein and hormone. Here we review current knowledge of PR post-translational modifications and discuss how these may influence receptor function focusing on human breast cancer cells. There is much left to be learned. However, our understanding of this may help to identify therapeutic agents that target PR activity in tissue-specific, even gene-specific ways.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsBreast NeoplasmsFemaleHumansMicePhosphorylationReceptors, ProgesteroneSumoylationUbiquitinationReceptors, ProgesteroneBreast cancerPhosphorylationPost-translational modificationProgesterone receptorSUMOylationTranscriptional activity

Identifiers

PMID24333793
PMCPMC3923415
OpenAlexW1996975584

What OpenQuestion holds

Textmetadata
LicenceTDM
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.