Evidence map›Paper›PMID 22433123›Full record

ReviewEndocrine reviews2012

Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.

Raj Kumar, Iain J McEwan

Open access · bronzeAbstract readReview
In one paragraph

Review in Endocrine reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
10.5field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 126 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
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  5. Review
  6. Article
  7. Article
  8. RXRActa pharmaceutica Sinica. B · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. All-Atomic Molecular Dynamic Studies of Human andInternational journal of molecular sciences · 2020
    Article
  16. NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Chemical Screening of Nuclear Receptor Modulators.International journal of molecular sciences · 2020
    Review
  18. Review
  19. Review
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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

2 authors at 1 institution in 2 countries.

Raj KumarDepartment of Basic Sciences, The Commonwealth Medical College, Scranton, Pennsylvania 18510, USA.
Iain J McEwan
Commonwealth Medical College · US

Funding

Structure:function studies of the glucocorticoid receptorR01DK058829 · NIDDK · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI KUMAR, RAJ · 2001 to 2007
$2.0M
Chief Scientist OfficeNIDDK NIH HHS R01 DK058829NIDDK NIH HHS R01DK058829
6 · The paper itself

Abstract

Steroid hormones are synthesized from cholesterol primarily in the adrenal gland and the gonads and play vital roles in normal physiology, the control of development, differentiation, metabolic homeostasis, and reproduction. The actions of these small lipophilic molecules are mediated by intracellular receptor proteins. It is just over 25 yr since the first cDNA for steroid receptors were cloned, a development that led to the birth of a superfamily of ligand-activated transcription factors: the nuclear receptors. The receptor proteins share structurally and functionally related ligand binding and DNA-binding domains but possess distinct N-terminal domains and hinge regions that are intrinsically disordered. Since the original cloning experiments, considerable progress has been made in our understanding of the structure, mechanisms of action, and biology of this important class of ligand-activated transcription factors. In recent years, there has been interest in the structural plasticity and function of the N-terminal domain of steroid hormone receptors and in the allosteric regulation of protein folding and function in response to hormone, DNA response element architecture, and coregulatory protein binding partners. The N-terminal domain can exist as an ensemble of conformers, having more or less structure, which prime this region of the receptor to rapidly respond to changes in the intracellular environment through hormone binding and posttranslation modifications. In this review, we address the question of receptor structure and function dynamics with particular emphasis on the structurally flexible N-terminal domain, intra- and interdomain communications, and the allosteric regulation of receptor action.

Indexed as

Gene Expression RegulationHumansLigandsModels, MolecularProtein ConformationReceptors, SteroidStructure-Activity RelationshipTranscription FactorsLigandsReceptors, SteroidTranscription Factors

Identifiers

PMID22433123
PMCPMC3596562
OpenAlexW2111652946

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.