Evidence map›Paper›PMID 15934135›Full record

ArticleThe EMBO journal2004

Transrepression by a liganded nuclear receptor via a bHLH activator through co-regulator switching.

Akiko Murayama, Mi-sun Kim, Junn Yanagisawa, Ken-ichi Takeyama, Shigeaki Kato

RetractedOpen access · greenAbstract readRetracted Publication
In one paragraph

Article in The EMBO journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.2field-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

40 citing papers in PubMed, 151 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. MDM2 binds and inhibits vitamin D receptor.Cell cycle (Georgetown, Tex.) · 2015
    Article
  7. Fundamentals of vitamin D hormone-regulated gene expression.The Journal of steroid biochemistry and molecular biology · 2014
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Vitamin D and the epigenome.Frontiers in physiology · 2014
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Akiko MurayamaInstitute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.
Mi-sun Kim
Junn Yanagisawa
Ken-ichi Takeyama
Shigeaki Kato
Institute of Applied Biochemistry · JPThe University of Tokyo · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vitamin D receptor (VDR) is essential for ligand-induced gene repression of 25(OH)D3 1alpha-hydroxylase (1alpha(OH)ase) in mammalian kidney, while this gene expression is activated by protein kinase A (PKA) signaling downstream of the parathyroid hormone action. The mapped negative vitamin D response element (1alphanVDRE) in the human 1alpha(OH)ase gene promoter (around 530 bp) was distinct from those of the reported DR3-like nVDREs, composed of two E-box-like motifs. Unlike the reported nVDREs, no direct binding of VDR/RXR heterodimer to 1alphanVDRE was detected. A bHLH-type factor, designated VDIR, was identified as a direct sequence-specific activator of 1nVDRE. The transactivation function of VDIR was further potentiated by activated-PKA signaling through phosphorylation of serine residues in the transactivation domains, with the recruitment of a p300 histone acetyltransferase co-activator. The ligand-dependent association of VDR/RXR heterodimer with VDIR bound to 1alphanVDRE caused the dissociation of p300 co-activators from VDIR, and the association of HDAC co-repressor complex components resulting in ligand-induced transrepression. Thus, the present study deciphers a novel mechanism of ligand-induced transrepression by nuclear receptor via co-regulator switching.

Indexed as

Gene Expression RegulationHelix-Loop-Helix MotifsVitamin D Response Element25-Hydroxyvitamin D3 1-alpha-HydroxylaseAmino Acid SequenceAnimalsBasic Helix-Loop-Helix ProteinsCell LineCyclic AMP-Dependent Protein KinasesE1A-Associated p300 ProteinHumansLigandsMiceMolecular Sequence DataNuclear ProteinsPromoter Regions, Genetic25-Hydroxyvitamin D3 1-alpha-HydroxylaseBasic Helix-Loop-Helix ProteinsCyclic AMP-Dependent Protein KinasesE1A-Associated p300 ProteinEp300 protein, mouseEp300 protein, ratLigandsNuclear ProteinsReceptors, CalcitriolRecombinant Fusion ProteinsRepressor ProteinsRetinoid X ReceptorsTcf3 protein, mouseTrans-ActivatorsTranscription Factors

Identifiers

PMID15934135
PMCPMC391066
OpenAlexW2060989542

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.