Evidence map›Paper›PMID 25765003›Full record

ArticleVirology2015

An unbiased proteomics approach to identify human cytomegalovirus RNA-associated proteins.

Erik M Lenarcic, Benjamin J Ziehr, Nathaniel J Moorman

Abstract read
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. RNA-targeted proteomics identifies YBX1 as critical for efficient HCMV mRNA translation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Crystal structure of the tegument protein UL82 (pp71) from human cytomegalovirus.Protein science : a publication of the Protein Society · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Expanding the Known Functional Repertoire of the Human Cytomegalovirus pp71 Protein.Frontiers in cellular and infection microbiology · 2020
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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.

Erik M LenarcicDepartment of Microbiology & Immunology, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, United States.
Benjamin J ZiehrDepartment of Microbiology & Immunology, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, United States.
Nathaniel J MoormanDepartment of Microbiology & Immunology, Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC, United States. Electronic address: nmoorman@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

The role of host and viral translation factors during HCMV infectionR01AI103311 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MOORMAN, NATHANIEL J · 2013 to 2022
$3.9M
NIAID NIH HHS 1R01AI103311-01NIAID NIH HHS R01 AI103311
6 · The paper itself

Abstract

Post-transcriptional events regulate herpesvirus gene expression, yet few herpesvirus RNA-binding proteins have been identified. We used an unbiased approach coupling oligo(dT) affinity capture with proteomics to identify viral RNA-associated proteins during infection. Using this approach, we identified and confirmed changes in the abundance or activity of two host RNA-associated proteins, DHX9 and DDX3, in cells infected with human cytomegalovirus (HCMV). We also identified and confirmed previously unreported activities for the HCMV US22 and pp71 proteins as RNA-associated viral proteins and confirmed that a known viral RNA-binding protein, pTRS1, associates with RNA in infected cells. Further, we found that HCMV pp71 co-sedimented with polysomes, associated with host and viral RNAs, and stimulated the overall rate of protein synthesis. These results demonstrate that oligo(dT) affinity capture coupled with proteomics provides a rapid and straightforward means to identify RNA-associated viral proteins during infection that may participate in the post-transcriptional control of gene expression.

Indexed as

ProteomicsCytomegalovirusCytomegalovirus InfectionsHumansMolecular Sequence DataProtein BiosynthesisRNA-Binding ProteinsRNA, ViralRNA-Binding ProteinsRNA, ViralHerpesvirusHuman cytomegalovirus (HCMV)Messenger RNA (mRNA)Post-transcriptional regulationProteomicsRNA-bindingTranslation

Identifiers

PMID25765003
PMCPMC4437878
OpenAlexW1974670748

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.