Evidence map›Paper›PMID 32461253›Full record

ArticleThe Journal of biological chemistry2020

Acyltransferase-mediated selection of the length of the fatty acyl chain and of the acylation site governs activation of bacterial RTX toxins.

Adriana Osickova, Humaira Khaliq, Jiri Masin, David Jurnecka, Anna Sukova, Radovan Fiser, Jana Holubova, Ondrej Stanek, Peter Sebo, Radim Osicka

Abstract 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Infective Endocarditis Due toMicroorganisms · 2024
    Review
  7. Article
  8. Microorganisms · 2022
    Review
  9. Microorganisms · 2022
    Review
  10. Ribosomally derived lipopeptides containing distinct fatty acyl moieties.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  11. Pathogenic determinants ofFrontiers in pediatrics · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Binding ofInternational journal of molecular sciences · 2020
    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

10 authors.

Adriana OsickovaInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Humaira KhaliqInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Jiri MasinInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
David JurneckaInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0002-1690-8908
Anna SukovaInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Radovan FiserInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Jana HolubovaInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Ondrej StanekInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.
Peter SeboInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic.ORCID 0000-0002-9755-7715
Radim OsickaInstitute of Microbiology of the Czech Academy of Sciences, Prague, Czech Republic osicka@biomed.cas.cz.ORCID 0000-0003-2626-5456

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a wide range of organisms, from bacteria to humans, numerous proteins have to be posttranslationally acylated to become biologically active. Bacterial

Indexed as

AcyltransferasesAnimalsBacteriaBacterial ProteinsCell LineFatty AcidsHemolysin ProteinsMiceAcyltransferasesBacterial ProteinsFatty AcidsHemolysin Proteinsacylationacyltransferaseadenylate cyclase toxin (CyaA)bacterial toxincytotoxicitycytotoxin (RtxA)fatty acidfatty acylposttranslational modificationprotein acylationprotein translocationprotoxinRTX toxinα-hemolysin (HlyA)

Identifiers

PMID32461253
PMCPMC7363117

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.