Evidence map›Paper›PMID 15858005›Full record

ArticleJournal of virology2005

Relocalization of the Mre11-Rad50-Nbs1 complex by the adenovirus E4 ORF3 protein is required for viral replication.

Jared D Evans, Patrick Hearing

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
5.7field-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

105 citing papers in PubMed, 151 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. The adenovirus DNA-binding protein DBP.Journal of virology · 2024
    Review
  8. SMC-based immunity against extrachromosomal DNA elements.Biochemical Society transactions · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Review

45 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.

Jared D EvansDepartment of Molecular Genetics and Microbiology, Stony Brook University School of Medicine, Stony Brook, New York 11794-5222, USA.
Patrick Hearing
Stony Brook University · US

Funding

TUMOR VIRUS-HOST INTERACTIONSP01CA028146 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1986 to 2005
$9.9M
VIRAL ONCOLOGYT32CA009176 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1985 to 2012
$5.2M
NCI NIH HHS CA09176NCI NIH HHS CA28146NCI NIH HHS P01 CA028146NCI NIH HHS T32 CA009176
6 · The paper itself

Abstract

Adenovirus replication is controlled by the relocalization or modification of nuclear protein complexes, including promyelocytic leukemia protein (PML) nuclear domains and the Mre11-Rad50-Nbs1 (MRN) DNA damage machinery. In this study, we demonstrated that the E4 ORF3 protein effects the relocalization of both PML and MRN proteins to similar structures within the nucleus at early times after infection. These proteins colocalize with E4 ORF3. Through the analysis of specific viral mutants, we found a direct correlation between MRN reorganization at early times after infection and the establishment of viral DNA replication domains. Further, the reorganization of MRN components may be uncoupled from the ability of E4 ORF3 to rearrange PML. At later stages of infection, components of the MRN complex disperse within the nucleus, Nbs1 is found within viral replication centers, Rad50 remains localized with E4 ORF3, and Mre11 is degraded. The importance of viral regulation of the MRN complex is underscored by the complementation of E4 mutant viruses in cells that lack Mre11 or Nbs1 activity. These results illustrate the importance of nuclear organization in virus growth and suggest that E4 ORF3 regulates activities in both PML nuclear bodies and the MRN complex to stimulate the viral replication program.

Indexed as

Acid Anhydride HydrolasesAdenoviridaeAdenovirus E4 ProteinsBiological TransportCell Cycle ProteinsCell NucleusDNA-Binding ProteinsDNA Repair EnzymesHumansMRE11 Homologue ProteinMultiprotein ComplexesNeoplasm ProteinsNuclear ProteinsOpen Reading FramesPromyelocytic Leukemia ProteinTime FactorsAcid Anhydride HydrolasesAdenovirus E4 ProteinsCell Cycle ProteinsDNA-Binding ProteinsDNA Repair EnzymesMRE11 Homologue ProteinMRE11 protein, humanMultiprotein ComplexesNBN protein, humanNeoplasm ProteinsNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinRAD50 protein, humanTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID15858005
PMCPMC1091726
OpenAlexW1999064296

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.