Evidence map›Paper›PMID 25512541›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Estrogen-related receptor α is required for efficient human cytomegalovirus replication.

Jesse Hwang, John G Purdy, Kai Wu, Joshua D Rabinowitz, Thomas Shenk

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Jesse HwangDepartments of Molecular Biology and.
John G PurdyChemistry and the Lewis-Sigler Institute for Integrative Genomics Princeton University, Princeton, NJ 08544.
Kai WuDepartments of Molecular Biology and.
Joshua D RabinowitzChemistry and the Lewis-Sigler Institute for Integrative Genomics Princeton University, Princeton, NJ 08544.
Thomas ShenkDepartments of Molecular Biology and tshenk@princeton.edu.
Princeton University · US

Funding

Mechanisms and consequences of metabolic manipulation by human cytomegalovirusR01AI097382 · NIAID · PRINCETON UNIVERSITY · PI RABINOWITZ, JOSHUA D, SHENK, THOMAS E · 2012 to 2015
$2.2M
NIAID NIH HHS R01 AI097382
6 · The paper itself

Abstract

An shRNA-mediated screen of the 48 human nuclear receptor genes identified multiple candidates likely to influence the production of human cytomegalovirus in cultured human fibroblasts, including the estrogen-related receptor α (ERRα), an orphan nuclear receptor. The 50-kDa receptor and a 76-kDa variant were induced posttranscriptionally following infection. Genetic and pharmacological suppression of the receptor reduced viral RNA, protein, and DNA accumulation, as well as the yield of infectious progeny. In addition, RNAs encoding multiple metabolic enzymes, including enzymes sponsoring glycolysis (enolase 1, triosephosphate isomerase 1, and hexokinase 2), were reduced when the function of ERRα was inhibited in infected cells. Consistent with the effect on RNAs, a substantial number of metabolites, which are normally induced by infection, were either not increased or were increased to a reduced extent in the absence of normal ERRα activity. We conclude that ERRα is needed for the efficient production of cytomegalovirus progeny, and we propose that the nuclear receptor contributes importantly to the induction of a metabolic environment that supports optimal cytomegalovirus replication.

Indexed as

Biomarkers, TumorCell LineCytomegalovirusCytomegalovirus InfectionsDNA-Binding ProteinsEstrogen Receptor alphaGlycolysisHexokinaseHumansPhosphopyruvate HydrataseProtein BiosynthesisRNA, ViralTriose-Phosphate IsomeraseTumor Suppressor ProteinsVirus ReplicationBiomarkers, TumorDNA-Binding ProteinsENO1 protein, humanESR1 protein, humanEstrogen Receptor alphaHexokinasePhosphopyruvate HydrataseRNA, ViralTriose-Phosphate IsomeraseTumor Suppressor Proteinsherpesvirusmass spectrometrymetabolismnuclear receptor

Identifiers

PMID25512541
PMCPMC4284536
OpenAlexW1987132818

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.