Evidence map›Paper›PMID 30654005›Full record

ReviewMolecular and cellular endocrinology2019

Alternative binding sites at the vitamin D receptor and their ligands.

Tania R Mutchie, Olivia B Yu, Elliot S Di Milo, Leggy A Arnold

Open access · greenAbstract readReview
In one paragraph

Review in Molecular and cellular endocrinology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. Vitamin DTurkish journal of medical sciences · 2024
    Article
  4. Review
  5. Demystifying the Functional Role of Nuclear Receptors in Esophageal Cancer.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Review
  8. Article
  9. Steroid receptor/coactivator binding inhibitors: An update.Molecular and cellular endocrinology · 2019
    Review
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

4 authors at 1 institution in 1 country.

Tania R MutchieDepartment of Chemistry and Biochemistry and Milwaukee Institute for Drug Discovery (MIDD), University of Wisconsin, Milwaukee, WI, 53211, USA.
Olivia B YuDepartment of Chemistry and Biochemistry and Milwaukee Institute for Drug Discovery (MIDD), University of Wisconsin, Milwaukee, WI, 53211, USA.
Elliot S Di MiloDepartment of Chemistry and Biochemistry and Milwaukee Institute for Drug Discovery (MIDD), University of Wisconsin, Milwaukee, WI, 53211, USA.
Leggy A ArnoldDepartment of Chemistry and Biochemistry and Milwaukee Institute for Drug Discovery (MIDD), University of Wisconsin, Milwaukee, WI, 53211, USA. Electronic address: arnold2@uwm.edu.
University of Wisconsin–Milwaukee · US

Funding

Small molecule inhibitors of the vitamin D receptor-coactivator interactionR03DA031090 · NIDA · UNIVERSITY OF WISCONSIN MILWAUKEE · PI ARNOLD, ALEXANDER · 2010 to 2011
$73k
NIDA NIH HHS R03 DA031090
6 · The paper itself

Abstract

In recent decades, the majority of ligands developed for the vitamin D receptor (VDR) bind at its deeply buried genomic ligand binding pocket. Theses ligands can be categorized into agonists and partial agonists/antagonists. A limited number of ligands, most of them peptides, bind the VDR‒coactivator binding site that is formed in the presence of an agonist and inhibit coactivator recruitment, and therefore transcription. Another solvent exposed VDR‒ligand binding pocket was identified for lithocholic acid, improving the overall stability of the VDR complex. Additional proposed interactions with VDR are discussed herein that include the alternative VDR‒ligand binding pocket that may mediate both non-genomic cellular responses and binding function 3 that was identified for the androgen receptor. Many VDR ligands increase blood calcium levels at therapeutic concentrations in vivo, thus the identification of alternative VDR‒ligand binding pockets might be crucial to develop non-calcemic and potent ligands for VDR to treat cancer and inflammatory disease.

Indexed as

AnimalsBinding SitesCalciumHumansLigandsModels, MolecularPeptidesProtein BindingProtein Structure, TertiaryReceptors, CalcitriolStructure-Activity RelationshipCalciumLigandsPeptidesReceptors, CalcitriolVDR protein, human1,25(OH)(2)D(3)Alternative VDR‒Binding function 3Coactivator inhibitorLigandLigand binding pocketVDR‒Vitamin D receptor

Identifiers

PMID30654005
PMCPMC6444937
OpenAlexW2909952250

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.