Evidence map›Paper›PMID 32019147›Full record

ArticleBiomolecules2020

Structural Determinants Responsible for the Preferential Insertion of Ribonucleotides by Bacterial NHEJ PolDom.

Alejandro Sánchez-Salvador, Miguel de Vega

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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.

Alejandro Sánchez-SalvadorCentro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Nicolás Cabrera, 1, 28049 Madrid, Spain.
Miguel de VegaCentro de Biología Molecular Severo Ochoa (Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid), Nicolás Cabrera, 1, 28049 Madrid, Spain.
Consejo Superior de Investigaciones Científicas · ES

Funding

Ministerio de Ciencia, Innovación y Universidades BFU2017-83900-P
6 · The paper itself

Abstract

The catalytic active site of the Polymerization Domain (PolDom) of bacterial Ligase D is designed to promote realignments of the primer and template strands and extend mispaired 3' ends. These features, together with the preferred use of ribonucleotides (

Indexed as

Amino Acid SequenceBacterial ProteinsCatalytic DomainDNA Breaks, Double-StrandedDNA-Directed DNA PolymeraseDNA End-Joining RepairDNA RepairGuanosine TriphosphateHistidineKineticsLigasesLysineMutagenesis, Site-DirectedMutationNucleotidesProtein BindingBacterial ProteinsDNA-Directed DNA PolymeraseGuanosine TriphosphateHistidineLigasesLysineNucleotidesRibonucleotidesThreoninearchaea/eukaryotic primaseDNA repairligase Dnonhomologous end joining (NHEJ)

Identifiers

PMID32019147
PMCPMC7072297
OpenAlexW3004222971

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.