Evidence map›Paper›PMID 30718611›Full record

ArticleScientific reports2019

Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding.

Magdalena Plotka, Enea Sancho-Vaello, Sebastian Dorawa, Anna-Karina Kaczorowska, Lukasz P Kozlowski, Tadeusz Kaczorowski, Kornelius Zeth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Engineered endolysin ofFrontiers in microbiology · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Molecular Characterization of a DNA Polymerase fromInternational journal of molecular sciences · 2022
    Article
  15. Article
  16. Article
  17. The Antibacterial Effect of PEGylated Carbosilane Dendrimers onInternational journal of molecular sciences · 2022
    Article
  18. Article
  19. Characterization ofFrontiers in microbiology · 2022
    Article
  20. Novel Lytic Enzyme of Prophage Origin fromInternational journal of molecular sciences · 2021
    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

7 authors at 4 institutions in 3 countries.

Magdalena PlotkaLaboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, Gdansk, Poland. magdalena.plotka@biol.ug.edu.pl.ORCID 0000-0002-2871-8060
Enea Sancho-VaelloUnidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Científicas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC,UPV/EHU), Leioa, Bizkaia, Spain.
Sebastian DorawaLaboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, Gdansk, Poland.
Anna-Karina KaczorowskaCollection of Plasmids and Microorganisms, Faculty of Biology, University of Gdansk, Gdansk, Poland.
Lukasz P KozlowskiInstitute of Informatics, Faculty of Mathematics, Informatics and Mechanics, University of Warsaw, Warsaw, Poland.
Tadeusz KaczorowskiLaboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, Gdansk, Poland. tadeusz.kaczorowski@biol.ug.edu.pl.
Kornelius ZethDepartment of Science and Environment, Roskilde University, Roskilde, Denmark.
University of Gdańsk · PLConsejo Superior de Investigaciones Científicas · ESRoskilde University · DKUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To escape from hosts after completing their life cycle, bacteriophages often use endolysins, which degrade bacterial peptidoglycan. While mesophilic phages have been extensively studied, their thermophilic counterparts are not well characterized. Here, we present a detailed analysis of the structure and function of Ts2631 endolysin from thermophilic phage vB_Tsc2631, which is a zinc-dependent amidase. The active site of Ts2631 consists of His30, Tyr58, His131 and Cys139, which are involved in Zn

Indexed as

BacteriolysisBacteriophagesCatalytic DomainEndopeptidasesModels, MolecularPeptidoglycanProtein ConformationThermusViral ProteinsendolysinEndopeptidasesPeptidoglycanViral Proteins

Identifiers

PMID30718611
PMCPMC6361986
OpenAlexW2914687836

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.