Evidence map›Paper›PMID 27380371›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Structure of a double hexamer of the Pyrococcus furiosus minichromosome maintenance protein N-terminal domain.

Martin Meagher, Eric J Enemark

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

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact, top 96% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024
    Review
  2. Review
  3. 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

2 authors at 1 institution in 1 country.

Martin MeagherDepartment of Structural Biology, St Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.
Eric J EnemarkDepartment of Structural Biology, St Jude Children's Research Hospital, 262 Danny Thomas Place, Memphis, TN 38105, USA.
St. Jude Children's Research Hospital · US

Funding

Molecular mechanisms of DNA replicationR01GM098771 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI ENEMARK, ERIC · 2011 to 2019
$3.1M
NIGMS NIH HHS R01 GM098771
6 · The paper itself

Abstract

The crystal structure of the N-terminal domain of the Pyrococcus furiosus minichromosome maintenance (MCM) protein as a double hexamer is described. The MCM complex is a ring-shaped helicase that unwinds DNA at the replication fork of eukaryotes and archaea. Prior to replication initiation, the MCM complex assembles as an inactive double hexamer at specific sites of DNA. The presented structure is highly consistent with previous MCM double-hexamer structures and shows two MCM hexamers with a head-to-head interaction mediated by the N-terminal domain. Minor differences include a diminished head-to-head interaction and a slightly reduced inter-hexamer rotation.

Indexed as

Amino Acid SequenceArchaeal ProteinsBinding SitesCations, DivalentCloning, MolecularCrystallography, X-RayDNA, ArchaealDNA ReplicationEscherichia coliGene ExpressionKineticsMinichromosome Maintenance ProteinsModels, MolecularPlasmidsProtein BindingProtein Conformation, alpha-HelicalArchaeal ProteinsCations, DivalentDNA, ArchaealMinichromosome Maintenance ProteinsRecombinant ProteinsZincDNA replicationhelicaseMCMminichromosome maintenancePyrococcus furiosus

Identifiers

PMID27380371
PMCPMC4933004
OpenAlexW2474924889

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.