Evidence map›Paper›PMID 31953321›Full record

ArticleThe Journal of biological chemistry2020

Functional interactions between gyrase subunits are optimized in a species-specific manner.

Daniela Weidlich, Dagmar Klostermeier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. AssessingbioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Comparative analysis ofFood chemistry: X · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Antibiotic Resistance and Mechanisms of Pathogenic Bacteria in Tubo-Ovarian Abscess.Frontiers in cellular and infection microbiology · 2022
    Review
  11. Review
  12. Article
  13. Review
  14. 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

2 authors at 1 institution in 1 country.

Daniela WeidlichInstitute for Physical Chemistry, University of Muenster, Corrensstrasse 30, D-48149 Muenster, Germany.
Dagmar KlostermeierInstitute for Physical Chemistry, University of Muenster, Corrensstrasse 30, D-48149 Muenster, Germany. Electronic address: dagmar.klostermeier@uni-muenster.de.
University of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA gyrase is a bacterial DNA topoisomerase that catalyzes ATP-dependent negative DNA supercoiling and DNA decatenation. The enzyme is a heterotetramer comprising two GyrA and two GyrB subunits. Its overall architecture is conserved, but species-specific elements in the two subunits are thought to optimize subunit interaction and enzyme function. Toward understanding the roles of these different elements, we compared the activities of

Indexed as

Adenosine TriphosphatasesBacteriaDNA, BacterialDNA GyraseDNA, SuperhelicalKineticsModels, MolecularProtein BindingProtein MultimerizationProtein SubunitsSpecies SpecificityStructural Homology, ProteinAdenosine TriphosphatasesDNA, BacterialDNA GyraseDNA, SuperhelicalProtein SubunitsATPasedecatenationDNA binding proteinDNA gyraseDNA-protein interactionDNA topoisomerasegenome integrityGyrAGyrBheterologous protein-protein interactionspecies specificitysubunit interactionsupercoiling mechanism

Identifiers

PMID31953321
PMCPMC7039563
OpenAlexW3000049205

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.