Evidence map›Paper›PMID 25490152›Full record

ArticleeLife2014

Architecture of the ring formed by the tubulin homologue FtsZ in bacterial cell division.

Piotr Szwedziak, Qing Wang, Tanmay A M Bharat, Matthew Tsim, Jan Löwe

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing papers in PubMed
19.6field-weighted citation impact, top 1% 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

129 citing papers in PubMed, 261 citations in OpenAlex.

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  10. Combining live fluorescence imaging with in situ cryoelectron tomography sheds light on the septation process inProceedings of the National Academy of Sciences of the United States of America · 2025
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69 more citing papers are in PubMed but not listed here.

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.

Piotr SzwedziakStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Qing WangStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Tanmay A M BharatStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Matthew TsimStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
Jan LöweStructural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.
MRC Laboratory of Molecular Biology · GB

Funding

Department of Health U105184326Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust 095514Wellcome Trust 095514/Z/11/Z
6 · The paper itself

Abstract

Membrane constriction is a prerequisite for cell division. The most common membrane constriction system in prokaryotes is based on the tubulin homologue FtsZ, whose filaments in E. coli are anchored to the membrane by FtsA and enable the formation of the Z-ring and divisome. The precise architecture of the FtsZ ring has remained enigmatic. In this study, we report three-dimensional arrangements of FtsZ and FtsA filaments in C. crescentus and E. coli cells and inside constricting liposomes by means of electron cryomicroscopy and cryotomography. In vivo and in vitro, the Z-ring is composed of a small, single-layered band of filaments parallel to the membrane, creating a continuous ring through lateral filament contacts. Visualisation of the in vitro reconstituted constrictions as well as a complete tracing of the helical paths of the filaments with a molecular model favour a mechanism of FtsZ-based membrane constriction that is likely to be accompanied by filament sliding.

Indexed as

Cell DivisionBacterial ProteinsCaulobacter crescentusCell MembraneCryoelectron MicroscopyCytoskeletal ProteinsEscherichia coliEscherichia coli ProteinsGene ExpressionLiposomesProtein Structure, SecondaryProtein Structure, TertiaryBacterial ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, E coliFtsZ protein, BacteriaLiposomesbacterial cytoskeletonC. crescentuscell biologycell divisioncytokinesisE. colielectron tomographyFtsZinfectious diseasemicrobiology

Identifiers

PMID25490152
PMCPMC4383033
OpenAlexW2168162456

What OpenQuestion holds

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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.