Evidence map›Paper›PMID 25528417›Full record

ArticleVirology2015

Structures of minute virus of mice replication initiator protein N-terminal domain: Insights into DNA nicking and origin binding.

Sunil K Tewary, Lingfei Liang, Zihan Lin, Annie Lynn, Susan F Cotmore, Peter Tattersall, Haiyan Zhao, Liang Tang

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Distinct evolutionary patterns of endemic and emerging parvoviruses and the origin of a new pandemic virus.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

8 authors at 2 institutions in 1 country.

Sunil K TewaryDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Lingfei LiangDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Zihan LinDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Annie LynnDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA.
Susan F CotmoreDepartments of Laboratory Medicine, Yale University Medical School, New Haven, CT 06510, USA.
Peter TattersallDepartments of Laboratory Medicine, Yale University Medical School, New Haven, CT 06510, USA; Departments of Genetics, Yale University Medical School, New Haven, CT 06510, USA.
Haiyan ZhaoDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA. Electronic address: zhaohy@ku.edu.
Liang TangDepartment of Molecular Biosciences, University of Kansas, Lawrence, KS 66045, USA. Electronic address: tangl@ku.edu.
University of Kansas · USYale University · US

Funding

Molecular Genetics of Parvoviral DNA ReplicationR37AI026109 · NIAID · YALE UNIVERSITY · PI TATTERSALL, PETER J. · 2009 to 2018
$5.4M
Genome packaging in DNA virusesR01GM090010 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI TANG, LIANG · 2010 to 2014
$1.3M
NIAID NIH HHS R37 AI026109NIAID NIH HHS R37AI026109NIGMS NIH HHS R01 GM090010NIGMS NIH HHS R01GM090010
6 · The paper itself

Abstract

Members of the Parvoviridae family all encode a non-structural protein 1 (NS1) that directs replication of single-stranded viral DNA, packages viral DNA into capsid, and serves as a potent transcriptional activator. Here we report the X-ray structure of the minute virus of mice (MVM) NS1 N-terminal domain at 1.45Å resolution, showing that sites for dsDNA binding, ssDNA binding and cleavage, nuclear localization, and other functions are integrated on a canonical fold of the histidine-hydrophobic-histidine superfamily of nucleases, including elements specific for this Protoparvovirus but distinct from its Bocaparvovirus or Dependoparvovirus orthologs. High resolution structural analysis reveals a nickase active site with an architecture that allows highly versatile metal ligand binding. The structures support a unified mechanism of replication origin recognition for homotelomeric and heterotelomeric parvoviruses, mediated by a basic-residue-rich hairpin and an adjacent helix in the initiator proteins and by tandem tetranucleotide motifs in the replication origins.

Indexed as

DNA Breaks, Single-StrandedAnimalsBase SequenceDNA HelicasesDNA ReplicationMiceMinute Virus of MiceModels, MolecularParvoviridae InfectionsProtein BindingProtein Structure, TertiaryReplication OriginRodent DiseasesTrans-ActivatorsViral Nonstructural ProteinsViral ProteinsDNA Helicasesreplication initiator proteinTrans-ActivatorsViral Nonstructural ProteinsViral ProteinsDNA replicationNickaseNon-structural protein 1NucleaseParvovirusSite-specific DNA binding

Identifiers

PMID25528417
PMCPMC4699654
OpenAlexW2123497560

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.