Evidence map›Paper›PMID 31390324›Full record

ReviewMicrobiology (Reading, England)2020

A highly processive actinobacterial topoisomerase I - thoughts on

Marcin J Szafran, Agnieszka Strzałka, Dagmara Jakimowicz

Open access · hybridAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Microbiology (Reading, England), 2020. 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
0.2field-weighted citation impact, top 47% 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, 4 citations in OpenAlex.

  1. Mechanistic basis for relaxation of DNA supercoils by human topoisomerase IIIα-RMI1-RMI2.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Review
  4. 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

3 authors at 1 institution in 1 country.

Marcin J SzafranLaboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Agnieszka StrzałkaLaboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Dagmara JakimowiczLaboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
University of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Topoisomerase I (TopA) is an essential enzyme that is required to remove excess negative supercoils from chromosomal DNA. Actinobacteria encode unusual TopA homologues with a unique C-terminal domain that contains lysine repeats and confers high enzyme processivity. Interestingly, the longest stretch of lysine repeats was identified in TopA from

Indexed as

ActinobacteriaBacterial ProteinsChromosomes, BacterialDNA, BacterialDNA, SuperhelicalDNA Topoisomerases, Type IGene Expression Regulation, BacterialLysineProtein DomainsStreptomycesBacterial ProteinsDNA, BacterialDNA, SuperhelicalDNA Topoisomerases, Type ILysinechromosome topologyStreptomycestopoisomerase I

Identifiers

PMID31390324
PMCPMC7398561
OpenAlexW2966317797

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.