Evidence map›Paper›PMID 35435730›Full record

ArticleJournal of virology2022

High-Resolution Structure of the Nuclease Domain of the Human Parvovirus B19 Main Replication Protein NS1.

Jonathan L Sanchez, Niloofar Ghadirian, Nancy C Horton

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

Article in Journal of virology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structures and implications of the nuclease domain of human parvovirus B19 NS1 protein.Computational and structural biotechnology journal · 2022
    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

3 authors at 1 institution in 1 country.

Jonathan L SanchezBMCB Graduate Program, University of Arizonagrid.134563.6, Tucson, Arizona, USA.ORCID 0000-0003-0097-465X
Niloofar GhadirianDepartment of Chemistry and Biochemistry, University of Arizonagrid.134563.6, Tucson, Arizona, USA.ORCID 0000-0002-3481-1560
Nancy C HortonDepartment of Molecular and Cellular Biology, University of Arizonagrid.134563.6, Tucson, Arizona, USA.ORCID 0000-0003-2710-8284
University of Arizona · US

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
GRADUATE TRAINING IN BIOCHEMISTRY AND MOLECULAR BIOLOGYT32GM008659 · NIGMS · UNIVERSITY OF ARIZONA · PI CAPALDI, ANDREW PAUL, WEINERT, TED A. · 1997 to 2019
$5.3M
NIGMS NIH HHS P30 GM133894NIGMS NIH HHS T32 GM008659
6 · The paper itself

Abstract

Two new structures of the N-terminal domain of the main replication protein, NS1, of human parvovirus B19 (B19V) are presented here. This domain (NS1-nuc) plays an important role in the "rolling hairpin" replication of the single-stranded B19V DNA genome, recognizing origin of replication sequences in double-stranded DNA, and cleaving (i.e., nicking) single-stranded DNA at a nearby site known as the terminal resolution site (trs). The three-dimensional structure of NS1-nuc is well conserved between the two forms, as well as with a previously solved structure of a sequence variant of the same domain; however, it is shown here at a significantly higher resolution (2.4 Å). Using structures of NS1-nuc homologues bound to single- and double-stranded DNA, models for DNA recognition and nicking by B19V NS1-nuc are presented that predict residues important for DNA cleavage and for sequence-specific recognition at the viral origin of replication.

Indexed as

Models, MolecularParvovirus B19, HumanViral Nonstructural ProteinsDNA, ViralEndonucleasesHumansProtein DomainsProtein Structure, TertiaryVirus ReplicationDNA, ViralEndonucleasesNS1 protein, parvovirusViral Nonstructural ProteinsDNA cleavageDNA nickingdouble-stranded DNA bindingendonucleaseenzymehuman parvovirus B19nucleaseparvovirusprotein structureprotein structure-functionsingle-stranded DNA bindingviral origin of replication

Identifiers

PMID35435730
PMCPMC9093113
OpenAlexW4225853013

What Socratic 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 Socratic graph.