Evidence map›Paper›PMID 21123381›Full record

ArticleJournal of virology2011

Export of adenoviral late mRNA from the nucleus requires the Nxf1/Tap export receptor.

Gayatri Yatherajam, Wenying Huang, S J Flint

Abstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Multiple nuclear-replicating viruses require the stress-induced protein ZC3H11A for efficient growth.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. DNA virus replication compartments.Journal of virology · 2014
    Review
  15. Review
  16. Review
  17. Tinkering with translation: protein synthesis in virus-infected cells.Cold Spring Harbor perspectives in biology · 2013
    Review
  18. Article
  19. Review
  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.

Gayatri YatherajamDepartment of Molecular Biology, Princeton University, Princeton, New Jersey 08854, USA.
Wenying Huang
S J Flint

Funding

Molecular Functions of the Adenoviral E1B 55 kDa ProteinR01AI058172 · NIAID · PRINCETON UNIVERSITY · PI FLINT, SARAH JANE · 2004 to 2008
$1.9M
NIAID NIH HHS R01 AI058172NIAID NIH HHS R01AI058172
6 · The paper itself

Abstract

One important function of the human adenovirus E1B 55-kDa protein is induction of selective nuclear export of viral late mRNAs. This protein interacts with the viral E4 Orf6 and four cellular proteins to form an infected-cell-specific E3 ubiquitin ligase. The assembly of this enzyme is required for efficient viral late mRNA export, but neither the relevant substrates nor the cellular pathway that exports viral late mRNAs has been identified. We therefore examined the effects on viral late gene expression of inhibition of the synthesis or activity of the mRNA export receptor Nxf1, which was observed to colocalize with the E1B 55-kDa protein in infected cells. When production of Nxf1 was impaired by using RNA interference, the efficiency of viral late mRNA export was reduced to a corresponding degree. Furthermore, synthesis of a dominant-negative derivative of Nxf1 during the late phase of infection interfered with production of a late structural protein. These observations indicate that the Nxf1 pathway is responsible for export of viral late mRNAs. As the infected-cell-specific E3 ubiquitin ligase targets its known substrates for proteasomal degradation, we compared the concentrations of several components of this pathway (Nxf1, Thox1, and Thoc4) in infected cells that did or did not contain this enzyme. Although the concentration of a well-established substrate, Mre11, decreased significantly in cells infected by adenovirus type 5 (Ad5), but not in those infected by the E1B 55-kDa protein-null mutant Hr6, no E1B 55-kDa protein-dependent degradation of the Nxf1 pathway proteins was observed.

Indexed as

Gene Expression Regulation, ViralActive Transport, Cell NucleusAdenovirus E1B ProteinsAdenovirus E4 ProteinsAdenoviruses, HumanCell NucleusHeLa CellsHumansNucleocytoplasmic Transport ProteinsRNA-Binding ProteinsRNA InterferenceRNA, MessengerRNA, ViralAdenovirus E1B ProteinsAdenovirus E4 ProteinsNucleocytoplasmic Transport ProteinsNXF1 protein, humanRNA-Binding ProteinsRNA, MessengerRNA, Viral

Identifiers

PMID21123381
PMCPMC3028892

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.