Evidence map›Paper›PMID 12626683›Full record

ReviewMicrobiology and molecular biology reviews : MMBR2003

Cytokinesis in bacteria.

Jeffery Errington, Richard A Daniel, Dirk-Jan Scheffers

Open access · greenAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 262 papers.

0numbers the graph read from it
0cells of the map it votes in
262citing papers in PubMed
20.2field-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

262 citing papers in PubMed, 602 citations in OpenAlex.

  1. Article
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  6. Review
  7. Article
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  9. Review
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  14. Expression of bovine annexin A4 inBiochemistry and biophysics reports · 2023
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Transcriptome of Epibiont SaccharibacteriaJournal of bacteriology · 2022
    Article
  20. Article

202 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

3 authors at 1 institution in 1 country.

Jeffery ErringtonSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom. jeff.errington@path.ox.ac.uk
Richard A Daniel
Dirk-Jan Scheffers
University of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Work on two diverse rod-shaped bacteria, Escherichia coli and Bacillus subtilis, has defined a set of about 10 conserved proteins that are important for cell division in a wide range of eubacteria. These proteins are directed to the division site by the combination of two negative regulatory systems. Nucleoid occlusion is a poorly understood mechanism whereby the nucleoid prevents division in the cylindrical part of the cell, until chromosome segregation has occurred near midcell. The Min proteins prevent division in the nucleoid-free spaces near the cell poles in a manner that is beginning to be understood in cytological and biochemical terms. The hierarchy whereby the essential division proteins assemble at the midcell division site has been worked out for both E. coli and B. subtilis. They can be divided into essentially three classes depending on their position in the hierarchy and, to a certain extent, their subcellular localization. FtsZ is a cytosolic tubulin-like protein that polymerizes into an oligomeric structure that forms the initial ring at midcell. FtsA is another cytosolic protein that is related to actin, but its precise function is unclear. The cytoplasmic proteins are linked to the membrane by putative membrane anchor proteins, such as ZipA of E. coli and possibly EzrA of B. subtilis, which have a single membrane span but a cytoplasmic C-terminal domain. The remaining proteins are either integral membrane proteins or transmembrane proteins with their major domains outside the cell. The functions of most of these proteins are unclear with the exception of at least one penicillin-binding protein, which catalyzes a key step in cell wall synthesis in the division septum.

Indexed as

Cytoskeletal ProteinsEscherichia coli ProteinsMuramoylpentapeptide CarboxypeptidasePeptidoglycan GlycosyltransferaseBacteriaBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCell DivisionCell MembraneHexosyltransferasesMembrane ProteinsMultienzyme ComplexesPenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesBacterial ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsEscherichia coli ProteinsFtsA protein, BacteriaFtsA protein, E coliFtsI protein, E coliFtsK protein, E coliftsL protein, E coliFtsN protein, E coliFtsQ protein, E coliFtsW protein, BacteriaFtsZ protein, BacteriaHexosyltransferasesMembrane ProteinsMultienzyme ComplexesMuramoylpentapeptide CarboxypeptidasePenicillin-Binding ProteinsPeptidoglycanPeptidoglycan GlycosyltransferasePeptidyl TransferasesZipA protein, E coli

Identifiers

PMID12626683
PMCPMC150516
OpenAlexW2115004879

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.