Evidence map›Paper›PMID 25188500›Full record

ArticlePloS one2014

Crystal structure of the mineralocorticoid receptor DNA binding domain in complex with DNA.

William H Hudson, Christine Youn, Eric A Ortlund

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

16 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. The glucocorticoid receptor potentiates aldosterone-induced transcription by the mineralocorticoid receptor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. The mineralocorticoid receptor forms higher order oligomers upon DNA binding.Protein science : a publication of the Protein Society · 2024
    Article
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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.

William H HudsonDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America; Discovery and Developmental Therapeutics, Winship Cancer Institute, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Christine YounDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America; Discovery and Developmental Therapeutics, Winship Cancer Institute, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Eric A OrtlundDepartment of Biochemistry, Emory University School of Medicine, Atlanta, Georgia, United States of America; Discovery and Developmental Therapeutics, Winship Cancer Institute, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Emory University · US

Funding

Graduate Training in the Pharmacological StudiesT32GM008602 · NIGMS · EMORY UNIVERSITY · PI HALL, RANDY A. · 1996 to 2021
$5.1M
American Heart Association-American Stroke Association 13PRE16920012NIGMS NIH HHS NIH 5T32GM008602-14NIGMS NIH HHS T32 GM008602
6 · The paper itself

Abstract

The steroid hormone receptors regulate important physiological functions such as reproduction, metabolism, immunity, and electrolyte balance. Mutations within steroid receptors result in endocrine disorders and can often drive cancer formation and progression. Despite the conserved three-dimensional structure shared among members of the steroid receptor family and their overlapping DNA binding preference, activation of individual steroid receptors drive unique effects on gene expression. Here, we present the first structure of the human mineralocorticoid receptor DNA binding domain, in complex with a canonical DNA response element. The overall structure is similar to the glucocorticoid receptor DNA binding domain, but small changes in the mode of DNA binding and lever arm conformation may begin to explain the differential effects on gene regulation by the mineralocorticoid and glucocorticoid receptors. In addition, we explore the structural effects of mineralocorticoid receptor DNA binding domain mutations found in type I pseudohypoaldosteronism and multiple types of cancer.

Indexed as

Amino Acid SequenceCrystallography, X-RayDNAEscherichia coliGene ExpressionHumansMolecular Sequence DataMutationNeoplasmsProtein Structure, SecondaryProtein Structure, TertiaryPseudohypoaldosteronismReceptors, GlucocorticoidReceptors, MineralocorticoidRecombinant ProteinsSequence AlignmentDNAReceptors, GlucocorticoidReceptors, MineralocorticoidRecombinant Proteins

Identifiers

PMID25188500
PMCPMC4154765
OpenAlexW2073027779

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.