Evidence map›Paper›PMID 11085922›Full record

ArticleThe Biochemical journal2000

All natural DR3-type vitamin D response elements show a similar functionality in vitro.

A Toell, P Polly, C Carlberg

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
4.0field-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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.

  1. Pooled it
  2. 1α,25(OH)(2)-Vitamin D3 increases dysferlin expression in vitro and in a human clinical trial.Molecular therapy : the journal of the American Society of Gene Therapy · 2012
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  8. No Association between Polymorphisms of Vitamin D and Oxytocin Receptor Genes and Autistic Spectrum Disorder in a Sample of Turkish Children.Clinical psychopharmacology and neuroscience : the official scientific journal of the Korean College of Neuropsychopharmacology · 2018
    Article
  9. Novel VDR antagonists based on the GW0742 scaffold.Bioorganic & medicinal chemistry letters · 2018
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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

3 authors at 1 institution in 1 country.

A ToellInstitut für Physiologische Chemie I and Biomedizinisches Forschungszentrum, Heinrich-Heine-Universität, Postfach 10 10 07, D-40001 Düsseldorf, Germany.
P Polly
C Carlberg
Heinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The vitamin D(3) receptor (VDR), which is the nuclear receptor for 1alpha,25-dihydroxyvitamin D(3) [1alpha,25(OH)(2)D(3)], acts primarily as a heterodimer with the retinoid X receptor (RXR) and binds preferentially to directly repeated arrangements of two hexameric binding sites with three spacing nucleotides [DR3-type vitamin D response elements (VDREs)]. In this study, all presently known natural DR3-type VDREs have been compared and classified on the basis of their complex-formation with VDR-RXR heterodimers and their ability to stabilize VDR-RXR heterodimer conformations. Based on the affinity of each VDRE for VDR-RXR heterodimers, the DR3-type VDREs were divided into three classes. The ligand sensitivity of this complex-formation and conformational stabilization was determined to be in the range of 0.1 nM. No significant differences in the 1alpha,25(OH)(2)D(3)-modulated interactions of the DR3-type VDRE-complexed VDR-RXR heterodimer with the co-activator SRC-1 (steroid receptor co-activator-1) or the co-repressor NCoR (nuclear receptor co-repressor) were found. Taken together, the affinity for VDR-RXR heterodimers appears to be the major discriminating parameter between natural DR3-type VDREs. This will not only facilitate further investigation of the principles of DR3-type-VDRE-mediated gene regulation, but also strongly suggests that DR3-type VDREs alone cannot explain the pleiotropic genomic action of 1alpha,25(OH)(2)D(3).

Indexed as

Base SequenceDimerizationHumansReceptors, CalcitriolReceptors, Retinoic AcidRetinoid X ReceptorsSignal TransductionTranscription FactorsReceptors, CalcitriolReceptors, Retinoic AcidRetinoid X ReceptorsTranscription Factors

Identifiers

PMID11085922
PMCPMC1221460
OpenAlexW2104829608

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.