Evidence map›Paper›PMID 25867546›Full record

ArticleProteomics2015

Human cytomegalovirus pUL97 kinase induces global changes in the infected cell phosphoproteome.

Adam Oberstein, David H Perlman, Thomas Shenk, Laura J Terry

Abstract read
In one paragraph

Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Cytomegalovirus disrupts Lamin A/C to control microtubule-mediated nuclear movement and cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  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

4 authors.

Adam ObersteinDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA.
David H PerlmanDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA.
Thomas ShenkDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA.
Laura J TerryDepartment of Molecular Biology, Princeton University, Princeton, NJ, USA.

Funding

Human cytomegalovirus-induced alterations to cell-surface adhesion proteinsR01AI112951 · NIAID · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 2015 to 2019
$1.8M
Human cytomegalovirus-induced alterations to cell-surface adhesion proteinsR56AI112951 · NIAID · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 2014 to 2014
$399k
Cell surface proteome of monocytes latently infected with human cytomegalovirusF32AI106175 · NIAID · PRINCETON UNIVERSITY · PI OBERSTEIN, ADAM LEE · 2014 to 2016
$175k
NIAID NIH HHS AI112951NIAID NIH HHS F32 AI106175NIAID NIH HHS F32AI106175-02NIAID NIH HHS R01 AI112951NIAID NIH HHS R56 AI112951
6 · The paper itself

Abstract

Replication of human cytomegalovirus (HCMV) is regulated in part by cellular kinases and the single viral Ser/Thr kinase, pUL97. The virus-coded kinase augments the replication of HCMV by enabling nuclear egress and altering cell cycle progression. These roles are accomplished through direct phosphorylation of nuclear lamins and the retinoblastoma protein, respectively. In an effort to identify additional pUL97 substrates, we analyzed the phosphoproteome of SILAC-labeled human fibroblasts during infection with either wild-type HCMV or a pUL97 kinase-dead mutant virus. Phosphopeptides were enriched over a titanium dioxide matrix and analyzed by high-resolution MS. We identified 157 unambiguous phosphosites from 106 cellular and 17 viral proteins whose phosphorylation required UL97. Analysis of peptides containing these sites allowed the identification of several candidate pUL97 phosphorylation motifs, including a completely novel phosphorylation motif, LxSP. Substrates harboring the LxSP motif were enriched in nucleocytoplasmic transport functions, including a number of components of the nuclear pore complex. These results extend the known functions of pUL97 and suggest that modulation of nuclear pore function may be important during HCMV replication.

Indexed as

Blotting, WesternCells, CulturedChromatography, LiquidCytomegalovirusCytomegalovirus InfectionsFibroblastsHumansPhosphoproteinsPhosphorylationPhosphotransferases (Alcohol Group Acceptor)Protein Interaction Domains and MotifsProteomeProteomicsTandem Mass SpectrometryVirus Replicationganciclovir kinasePhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)ProteomeCell biologyHerpesvirusHuman cytomegalovirusNuclear pore complexTREX complexViral kinase

Identifiers

PMID25867546
PMCPMC4522931

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.