Evidence map›Paper›PMID 33158165›Full record

ArticleCells2020

Functional Characterization of the

Tanja Küssau, Niël Van Wyk, Matt D Johansen, Husam M A B Alsarraf, Aymeric Neyret, Claire Hamela, Kasper K Sørensen, Mikkel B Thygesen, Claire Beauvineau, Laurent Kremer and 1 more

Abstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. The Ubiquitination ofBiology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Virulence Mechanisms ofFrontiers in microbiology · 2022
    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

11 authors.

Tanja KüssauInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.
Niël Van WykInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.ORCID 0000-0003-3031-8821
Matt D JohansenInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.ORCID 0000-0001-5553-5270
Husam M A B AlsarrafInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.
Aymeric NeyretCEMIPAI CNRS UM UMS3725, CEDEX 5, 34293 Montpellier, France.
Claire HamelaInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.
Kasper K SørensenDepartment of Chemistry, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.
Mikkel B ThygesenDepartment of Chemistry, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark.ORCID 0000-0002-0158-2802
Claire BeauvineauChemical Library Institut Curie/CNRS, CNRS UMR9187, INSERM U1196 and CNRS UMR3666, INSERM U1193, Université Paris-Saclay, F-91405 Orsay, France.
Laurent KremerInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.ORCID 0000-0002-6604-4458
Mickaël BlaiseInstitut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier, CNRS UMR 9004, CEDEX 5, 34293 Montpellier, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptidoglycan (PG) is made of a polymer of disaccharides organized as a three-dimensional mesh-like network connected together by peptidic cross-links. PG is a dynamic structure that is essential for resistance to environmental stressors. Remodeling of PG occurs throughout the bacterial life cycle, particularly during bacterial division and separation into daughter cells. Numerous autolysins with various substrate specificities participate in PG remodeling. Expression of these enzymes must be tightly regulated, as an excess of hydrolytic activity can be detrimental for the bacteria. In non-tuberculous mycobacteria such as

Indexed as

AnimalsCrystallography, X-RayDisease Models, AnimalEnzyme InhibitorsGene DeletionHumansLarvaMacrophagesMicrobial Sensitivity TestsMolecular Docking SimulationMycobacterium abscessusMycobacterium Infections, NontuberculousN-Acetylmuramoyl-L-alanine AmidasePhenotypeStructural Homology, ProteinTHP-1 CellsEnzyme InhibitorsN-Acetylmuramoyl-L-alanine Amidasedrug screeningMycobacterium abscessusN-acetylmuramyl-l-alanine amidasepeptidoglycanx-ray crystallography

Identifiers

PMID33158165
PMCPMC7694207

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.