Evidence map›Paper›PMID 28357277›Full record

ArticleMicrobial cell (Graz, Austria)2015

EzrA: a spectrin-like scaffold in the bacterial cell division machinery.

Robert Cleverley, Richard Lewis

Open access · goldAbstract readComment
In one paragraph

Article in Microbial cell (Graz, Austria), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 33% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Robert CleverleyInstitute for Cell and Molecular Biosciences, University of Newcastle, Newcastle-upon-Tyne, NE2 4HH, UK.
Richard LewisInstitute for Cell and Molecular Biosciences, University of Newcastle, Newcastle-upon-Tyne, NE2 4HH, UK.
Newcastle University · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G015902/1
6 · The paper itself

Abstract

Much progress has been made in identifying the components of the divisome, the assembly of proteins that undertakes the vital process of cell division in bacteria. However, how the highly interdependent processes on either side of the membrane are coordinated during division is a major unresolved question. How is the degradation and synthesis of the cell wall on the outside of the cell coordinated with cytokinesis and membrane fission, which are driven from the inside of the cell by the tubulin homologue FtsZ? A possible key mediator of such coordination is the membrane protein EzrA, as it interacts both with FtsZ and the penicillin binding proteins (PBPs) that synthesize peptidoglycan. Cleverley

Indexed as

cell divisioncrystallographycytoskeletonEzrAspectrin

Identifiers

PMID28357277
PMCPMC5354558
OpenAlexW2053094682

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.