Evidence map›Paper›PMID 11121054›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

UL82 virion protein activates expression of immediate early viral genes in human cytomegalovirus-infected cells.

W A Bresnahan, T E Shenk

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

119 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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
  5. Article
  6. The Pentamer glycoprotein complex inhibits viral Immediate Early transcription during Human Cytomegalovirus infections.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Computational modeling of protracted HCMV replication using genome substrates and protein temporal profiles.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. A molecular mechanism for probabilistic bet hedging and its role in viral latency.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

59 more citing papers are in PubMed but not listed here.

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 1 country.

W A BresnahanDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.
T E Shenk
Princeton University · US

Funding

HUMAN CYTOMEGALOVIRUS TEGUMENT PROTEINSR01CA082396 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 1999 to 2013
$5.0M
CHARACTERIZATION OF HUMAN CYTOMEGALOVIRUS VIRION RNAF32AI010448 · NIAID · PRINCETON UNIVERSITY · PI BRESNAHAN, WADE A · 2000 to 2001
$55k
NCI NIH HHS CA82396NCI NIH HHS R01 CA082396NIAID NIH HHS AI10448NIAID NIH HHS F32 AI010448
6 · The paper itself

Abstract

The human cytomegalovirus UL82 gene encodes a protein (pp71) that is localized in the tegument domain of the virus particle. The UL82 gene product is delivered to the nucleus at the time of infection, and it is believed to function in gene activation. We have constructed a human cytomegalovirus mutant, ADsubUL82, that lacks a substantial portion of the UL82 coding region. It was propagated on human diploid fibroblasts expressing the UL82 gene product, and it was possible to produce a mutant virus lacking the UL82 protein by passaging virus stocks for one cycle of growth on normal, noncomplementing fibroblasts. The UL82-deficient mutant displays a multiplicity-dependent growth defect in normal human fibroblasts. The growth of ADsubUL82 is severely restricted at low input multiplicities (0.01-0.1 plaque-forming units per cell), producing a yield that is reduced by a factor of about 10(5) in comparison to wild-type virus. At higher input multiplicities (10 plaque-forming units per cell), ADsubUL82 grew nearly as well as the wild-type virus. By using a human cytomegalovirus gene array, we demonstrated that UL82 functions to facilitate virus mRNA accumulation very early during the human cytomegalovirus replication cycle. The growth phenotype associated with the UL82 mutant seems to result from its inability to efficiently activate human cytomegalovirus immediate early genes.

Indexed as

Gene Expression Regulation, ViralAntigens, ViralCell LineCytomegalovirusHumansImmediate-Early ProteinsPhosphoproteinsTranscriptional ActivationViral ProteinsAntigens, Viralcytomegalovirus phosphoprotein 71kDaImmediate-Early Proteinsimmediate-early proteins, cytomegalovirusPhosphoproteinsViral Proteins

Identifiers

PMID11121054
PMCPMC18949
OpenAlexW2131468538

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.