Evidence map›Paper›PMID 9733839›Full record

ArticleJournal of virology1998

Biochemical activities of minute virus of mice nonstructural protein NS1 are modulated In vitro by the phosphorylation state of the polypeptide.

J P Nüesch, R Corbau, P Tattersall, J Rommelaere

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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Oncolytic H-1 Parvovirus Shows Safety and Signs of Immunogenic Activity in a First Phase I/IIa Glioblastoma Trial.Molecular therapy : the journal of the American Society of Gene Therapy · 2017
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  17. 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
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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.

J P NüeschDepartment of Applied Tumor Virology and Institut National de la Santé et de la Recherche Médicale U375, Deutsches Krebsforschungszentrum, Heidelberg, Germany. jpf.nuesch@dkfz-heidelberg.de
R Corbau
P Tattersall
J Rommelaere
DKFZ-ZMBH Alliance · DEGerman Cancer Research Center · DEYale University · US

Funding

Molecular Genetics of Parvoviral DNA ReplicationR37AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 2009 to 2018
$5.4M
MOLECULAR GENETICS OF PARVOVIRAL DNA REPLICATIONR01AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 1988 to 2009
$3.0M
NIAID NIH HHS AI26109NIAID NIH HHS R01 AI026109NIAID NIH HHS R37 AI026109
6 · The paper itself

Abstract

NS1, the 83-kDa major nonstructural protein of minute virus of mice (MVM), is a multifunctional nuclear phosphoprotein which is required in a variety of steps during progeny virus production, early as well as late during infection. NS1 is the initiator protein for viral DNA replication. It binds specifically to target DNA motifs; has site-specific single-strand nickase, intrinsic ATPase, and helicase activities; trans regulates viral and cellular promoters; and exerts cytotoxic stress on the host cell. To investigate whether these multiple activities of NS1 depend on posttranslational modifications, in particular phosphorylation, we expressed His-tagged NS1 in HeLa cells by using recombinant vaccinia viruses, dephosphorylated it at serine and threonine residues with calf intestine alkaline phosphatase, and compared the biochemical activities of the purified un(der)phosphorylated (NS1(O)) and the native (NS1(P)) polypeptides. Biochemical analyses of replicative functions of NS1(O) revealed a severe reduction of intrinsic helicase activity and, to a minor extent, of ATPase and nickase activities, whereas its affinity for the target DNA sequence [ACCA]2-3 was enhanced compared to that of NS1(P). In the presence of endogenous protein kinases found in replication extracts, NS1(O) showed all functions necessary for resolution and replication of the 3' dimer bridge, indicating reactivation of NS1(O) by rephosphorylation. Partial reactivation of the helicase activity was found as well when NS1(O) was incubated with protein kinase C.

Indexed as

Base SequenceDNA HelicasesDNA PrimersEnzyme ActivationHeLa CellsHumansMinute Virus of MicePhosphorylationViral Nonstructural ProteinsDNA HelicasesDNA PrimersNS1 protein, minute virus of miceViral Nonstructural Proteins

Identifiers

PMID9733839
PMCPMC110136
OpenAlexW2170143023

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.