Evidence map›Paper›PMID 18165305›Full record

ArticleJournal of bacteriology2008

The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.

Adeline Derouaux, Benoît Wolf, Claudine Fraipont, Eefjan Breukink, Martine Nguyen-Distèche, Mohammed Terrak

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 62 citations in OpenAlex.

  1. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
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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

6 authors at 2 institutions in 2 countries.

Adeline DerouauxCentre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, B6a, B-4000 Sart-Tilman (Liège), Belgium.
Benoît Wolf
Claudine Fraipont
Eefjan Breukink
Martine Nguyen-Distèche
Mohammed Terrak
University of Liège · BEUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN, suggesting that MtgA may play a role in peptidoglycan assembly during the cell cycle in collaboration with other proteins.

Indexed as

Bacterial ProteinsEscherichia coliEscherichia coli ProteinsGreen Fluorescent ProteinsMembrane ProteinsMicroscopy, FluorescencePenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseProtein BindingRecombinant Fusion ProteinsSerine-Type D-Ala-D-Ala CarboxypeptidaseTwo-Hybrid System TechniquesBacterial ProteinsEscherichia coli ProteinsFtsN protein, E coliFtsW protein, BacteriaGreen Fluorescent ProteinsMembrane Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseRecombinant Fusion ProteinsSerine-Type D-Ala-D-Ala Carboxypeptidase

Identifiers

PMID18165305
PMCPMC2258671
OpenAlexW2028328535

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.