Evidence map›Paper›PMID 9557665›Full record

ArticleJournal of virology1998

Two RING finger proteins, the oncoprotein PML and the arenavirus Z protein, colocalize with the nuclear fraction of the ribosomal P proteins.

K L Borden, E J Campbelldwyer, G W Carlile, M Djavani, M S Salvato

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

58 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Ribosomal control in RNA virus-infected cells.Frontiers in microbiology · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Nuclear domain 10 of the viral aspect.World journal of virology · 2013
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
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

5 authors at 2 institutions in 2 countries.

K L BordenDepartment of Biochemistry, Dalhousie University, Halifax, Nova Scotia, Canada. kathyb@inka.mssm.edu
E J Campbelldwyer
G W Carlile
M Djavani
M S Salvato
Dalhousie University · CAUniversity of Wisconsin–Madison · US

Funding

MOLECULAR BASIS OF ARENAVIRUS VIRULENCER01AI032107 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI SALVATO, MARIA S. · 1994 to 1996
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MOLECULAR DETERMINANTS OF THE CYTOTOXIC T CELL RESPONSER29AI025522 · NIAID · UNIVERSITY OF WISCONSIN MADISON · PI SALVATO, MARIA S. · 1988 to 1992
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NIAID NIH HHS R01 AI032107NIAID NIH HHS R01 AI32107NIAID NIH HHS R29 AI25522
6 · The paper itself

Abstract

The promyelocytic leukemia (PML) protein forms nuclear bodies which are relocated to the cytoplasm by the RNA virus lymphocytic choriomeningitis virus (LCMV). The viral Z protein directly binds to PML and can relocate the nuclear bodies. Others have observed that LCMV virions may contain ribosomes; hence, we investigated the effects of infection on the distribution of ribosomal P proteins (P0, P1, and P2) with PML as a reference point. We demonstrate an association of PML bodies with P proteins by indirect immunofluorescence and coimmunoprecipitation experiments, providing the first evidence of nucleic acid-binding proteins associated with PML bodies. We show that unlike PML, the P proteins are not redistributed upon infection. Immunofluorescence and coimmunoprecipitation studies indicate that the viral Z protein binds the nuclear, but not the cytoplasmic, fraction of P0. The nuclear fraction of P0 has been associated with translationally coupled DNA excision repair and with nonspecific endonuclease activity; thus, P0 may be involved in nucleic acid processing activities necessary for LCMV replication. During the infection process, PML, P1, and P2 are downregulated but P0 remains unchanged. Further, P0 is present in virions while PML is not, indicating some selectivity in the assembly of LCMV.

Indexed as

Protozoan ProteinsZinc Fingers3T3 CellsAnimalsCell FractionationCell LineCell NucleusCricetinaeCytoplasmHeLa CellsHumansLymphocytic choriomeningitis virusMiceNeoplasm ProteinsNuclear ProteinsPromyelocytic Leukemia ProteinL12E protein, Trypanosoma cruziNeoplasm ProteinsNuclear ProteinsPML protein, humanPml protein, mousePromyelocytic Leukemia ProteinProtozoan ProteinsRibosomal ProteinsTranscription FactorsTumor Suppressor ProteinsViral Proteins

Identifiers

PMID9557665
PMCPMC109605
OpenAlexW2110098007

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.