Evidence map›Paper›PMID 32022687›Full record

ArticleeLife2020

Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-

Allison Hillary Williams, Richard Wheeler, Ala-Eddine Deghmane, Ignacio Santecchia, Ryan E Schaub, Samia Hicham, Maryse Moya Nilges, Christian Malosse, Julia Chamot-Rooke, Ahmed Haouz and 4 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024
    Article
  2. Review
  3. Article
  4. Article
  5. Anti-Virulence Therapeutic Approaches forAntibiotics (Basel, Switzerland) · 2021
    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

14 authors at 6 institutions in 2 countries.

Allison Hillary WilliamsUnité Biologie et Génétique de la Paroi Bactérienne, Institut Pasteur; Groupe Avenir, INSERM 75015, Paris, France.ORCID 0000-0002-0726-141X
Richard WheelerUnité Biologie et Génétique de la Paroi Bactérienne, Institut Pasteur; Groupe Avenir, INSERM 75015, Paris, France.
Ala-Eddine DeghmaneUnité des Infection Bactériennes Invasives, Institut Pasteur, Paris, France.
Ignacio SantecchiaUnité Biologie et Génétique de la Paroi Bactérienne, Institut Pasteur; Groupe Avenir, INSERM 75015, Paris, France.
Ryan E SchaubDepartment of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, United States.
Samia HichamUnité Biologie et Génétique de la Paroi Bactérienne, Institut Pasteur; Groupe Avenir, INSERM 75015, Paris, France.
Maryse Moya NilgesUnité Technologie et Service BioImagerie Ultrastructural, Institut Pasteur, Paris, France.
Christian MalosseUnité Technologie et Service Spectrométrie de Masse pour la Biologie, Institut Pasteur; UMR 3528, CNRS 75015, Paris, France.
Julia Chamot-RookeUnité Technologie et Service Spectrométrie de Masse pour la Biologie, Institut Pasteur; UMR 3528, CNRS 75015, Paris, France.
Ahmed HaouzPlate-forme de Cristallographie-C2RT, Institut Pasteur; UMR3528, CNRS 75015, Paris, France.
Joseph P DillardDepartment of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, United States.
William P RobinsDepartment of Microbiology, Harvard Medical School, Boston, United States.
Muhamed-Kheir TahaUnité des Infection Bactériennes Invasives, Institut Pasteur, Paris, France.
Ivo Gomperts BonecaUnité Biologie et Génétique de la Paroi Bactérienne, Institut Pasteur; Groupe Avenir, INSERM 75015, Paris, France.
Inserm · FRCentre National de la Recherche Scientifique · FRInstitut Pasteur · FRUniversity of Wisconsin–Madison · USDélégation Paris 5 · FRHarvard University · US

Funding

Peptidoglycan metabolism and fragment releaseR01AI097157 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI DILLARD, JOSEPH P · 2012 to 2022
$5.6M
European Molecular Biology Organization ALTF 732-2010European Research Council PGN from SHAPE to VIR 202283Fondation pour la Recherche Médicale DBF20160635726Fondation pour la Recherche Médicale FDT201805005258Institut Carnot-Pasteur Maladies Infectious fellowshipNIAID NIH HHS R01 AI097157
6 · The paper itself

Abstract

Lytic transglycosylases (LT) are enzymes involved in peptidoglycan (PG) remodeling. However, their contribution to cell-wall-modifying complexes and their potential as antimicrobial drug targets remains unclear. Here, we determined a high-resolution structure of the LT, an outer membrane lipoprotein from

Indexed as

Amino Acid SequenceCatalytic DomainCell WallGlycosyltransferasesMorphogenesisNeisseria meningitidisPeptidoglycanProtein BindingGlycosyltransferasesPeptidoglycancell divisioncell separationE. coliinfectious diseaseLytic transglycosylasemicrobiologyNeisseria meningitidispeptidoglycanX-ray crystallography

Identifiers

PMID32022687
PMCPMC7083599
OpenAlexW3005378413

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.