Evidence map›Paper›PMID 35253642›Full record

ArticleMicrobiology (Reading, England)2022

Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces.

Caroline Pearson, Sarah Tindall, Jennifer R Potts, Gavin H Thomas, Marjan W van der Woude

Open access · hybridAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed, 1 pooled it
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

8 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.

  1. InferiorMicrobial genomics · 2024
    Pooled it
  2. AnResearch square · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
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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

5 authors at 1 institution in 1 country.

Caroline PearsonDepartment of Biology, University of York, Heslington, UK.
Sarah TindallDepartment of Biology, University of York, Heslington, UK.
Jennifer R PottsDepartment of Biology, University of York, Heslington, UK.
Gavin H ThomasDepartment of Biology, University of York, Heslington, UK.
Marjan W van der WoudeYork Biomedical Institute, University of York, Heslington, UK.
University of York · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M011151/1British Heart Foundation PG/16/5/31912
6 · The paper itself

Abstract

The acylation of sugars, most commonly via acetylation, is a widely used mechanism in bacteria that uses a simple chemical modification to confer useful traits. For structures like lipopolysaccharide, capsule and peptidoglycan, that function outside of the cytoplasm, their acylation during export or post-synthesis requires transport of an activated acyl group across the membrane. In bacteria this function is most commonly linked to a family of integral membrane proteins - acyltransferase-3 (AT3). Numerous studies examining production of diverse extracytoplasmic sugar-containing structures have identified roles for these proteins in

Indexed as

AcyltransferasesPeptidoglycanAcetylationAcylationBacteriaBacterial ProteinsAcyltransferasesBacterial ProteinsPeptidoglycanacetyl-CoAantibioticscapsuleexopolysaccharidelipopolysaccharidemembrane-bound acyltransferasemycolic acidnodulationO-acetylationO-succinylation

Identifiers

PMID35253642
PMCPMC9558356
OpenAlexW4220903297

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.