Evidence map›Paper›PMID 7559785›Full record

ArticleThe Journal of cell biology1995

Targeting of adenovirus E1A and E4-ORF3 proteins to nuclear matrix-associated PML bodies.

T Carvalho, J S Seeler, K Ohman, P Jordan, U Pettersson, G Akusjärvi, M Carmo-Fonseca, A Dejean

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.

0numbers the graph read from it
0cells of the map it votes in
144citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

144 citing papers in PubMed, 265 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. E4orf1 SuppressesVaccines · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Review

84 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

8 authors at 1 institution in 1 country.

T CarvalhoInstituto de Histologia, Faculdade de Medicina, Lisboa, Portugal.
J S Seeler
K Ohman
P Jordan
U Pettersson
G Akusjärvi
M Carmo-Fonseca
A Dejean
Instituto de Medicina Tropical · PY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PML protein was first identified as part of a fusion product with the retinoic acid receptor alpha (RAR alpha), resulting from the t(15;17) chromosomal translocation associated with acute promyelocytic leukemia (APL). It has been previously demonstrated that PML, which is tightly bound to the nuclear matrix, concentrates in discrete subnuclear compartments that are disorganized in APL cells due to the expression of the PML-RAR alpha hybrid. Here we report that adenovirus infection causes a drastic redistribution of PML from spherical nuclear bodies into fibrous structures. The product encoded by adenovirus E4-ORF3 is shown to be responsible for this reorganization and to colocalize with PML into these fibers. In addition, we demonstrate that E1A oncoproteins concentrate in the PML domains, both in infected and transiently transfected cells, and that this association requires the conserved amino acid motif (D)LXCXE, common to all viral oncoproteins that bind pRB or the related p107 and p130 proteins. The SV-40 large T antigen, another member of this oncoprotein family is also found in close association with the PML nuclear bodies. Taken together, the present data indicate that the subnuclear domains containing PML represent a preferential target for DNA tumor viruses, and therefore suggest a more general involvement of the PML nuclear bodies in oncogenic processes.

Indexed as

Neoplasm ProteinsNuclear ProteinsAdenovirus E1A ProteinsAdenovirus E4 ProteinsAmino Acid SequenceAntigens, Polyomavirus TransformingBacterial AdhesionBacterial ProteinsHeLa CellsHumansMicroscopy, ElectronMolecular Sequence DataNuclear MatrixOncogene ProteinsOpen Reading FramesPromyelocytic Leukemia ProteinAdenovirus E1A ProteinsAdenovirus E4 ProteinsAntigens, Polyomavirus TransformingBacterial ProteinsNeoplasm ProteinsNuclear ProteinsOncogene ProteinsPML protein, humanPromyelocytic Leukemia ProteinTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID7559785
PMCPMC2120608
OpenAlexW2139168442

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.