Evidence map›Paper›PMID 12477848›Full record

ArticleJournal of virology2003

Regulation of minute virus of mice NS1 replicative functions by atypical PKClambda in vivo.

Jürg P F Nüesch, Sylvie Lachmann, Romuald Corbau, Jean Rommelaere

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. 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
1.1field-weighted citation impact, top 21% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification and genomic characterization of bovine parvovirus 1 in yaks.Journal of veterinary diagnostic investigation : official publication of the American Association of Veterinary Laboratory Diagnosticians, Inc · 2021
    Article
  4. Review
  5. Article
  6. Article
  7. Viral genes as oncolytic agents for cancer therapy.Cellular and molecular life sciences : CMLS · 2015
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. A viral adaptor protein modulating casein kinase II activity induces cytopathic effects in permissive cells.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 3 institutions in 2 countries.

Jürg P F NüeschProgram of Applied Tumor Virology, Abteilung F0100, Deutsches Krebsforschungszentrum, Heidelberg, Germany. jpf.nuesch@dkfz-heidelberg.de
Sylvie Lachmann
Romuald Corbau
Jean Rommelaere
German Cancer Research Center · DEDKFZ-ZMBH Alliance · DEInstitute of Virology of the Slovak Academy of Sciences · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Minute virus of mice NS1 protein is a multifunctional phosphoprotein endowed with a variety of enzymatic and regulatory activities necessary for progeny virus particle production. To regulate all of its different functions in the course of a viral infection, NS1 has been proposed to be modulated by posttranslational modifications, in particular, phosphorylation. Indeed, it was shown that the NS1 phosphorylation pattern is altered during the infectious cycle and that the biochemical profile of the protein is dependent on the phosphorylation state of the polypeptide. Moreover, in vitro approaches have identified members of the protein kinase C (PKC) family, in particular, atypical PKC, as regulators of viral DNA replication through the phosphorylation of NS1 residues T435 and S473, thereby activating the protein for DNA unwinding activities. In order to substantiate these findings in vivo, we produced NS1 in the presence of a dominant-negative PKClambda mutant and characterized the purified protein in vitro. The NS1 protein produced under these conditions was found to be only partially phosphorylated and as a consequence to be deficient for viral DNA replication. However, it could be rescued for this viral function by treatment with recombinant activated PKClambda. Our data clearly demonstrate that NS1 is a target for PKClambda phosphorylation in vivo and that this modification is essential for the helicase activity of the viral polypeptide. In addition, the phosphorylation of NS1 at residues T435 and S473 appeared to occur mainly in the nucleus, providing further evidence for the involvement of PKClambda which, unlike PKCzeta, accumulates in the nuclear compartment of infected cells.

Indexed as

Virus ReplicationAnimalsCell NucleusCells, CulturedHumansIsoenzymesMinute Virus of MicePhosphorylationProtein Kinase CProtein Kinase C-lambdaProtein Kinase C-thetaViral Nonstructural ProteinsIsoenzymesNS1 protein, minute virus of micePRKCQ protein, humanProtein Kinase CProtein Kinase C-lambdaProtein Kinase C-thetaViral Nonstructural Proteins

Identifiers

PMID12477848
PMCPMC140590
OpenAlexW2156642438

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.