Evidence map›Paper›PMID 32907942›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

A conserved subcomplex within the bacterial cytokinetic ring activates cell wall synthesis by the FtsW-FtsI synthase.

Lindsey S Marmont, Thomas G Bernhardt

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
9.7field-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

58 citing papers in PubMed, 92 citations in OpenAlex.

  1. Defining the order of assembly of theJournal of bacteriology · 2026
    Article
  2. Article
  3. Control of cell division by anbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026
    Article
  6. A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Conformational regulation of two essential activators of bacterial cell elongation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  13. FtsZ-mediated spatial-temporal control over septal cell wall synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

2 authors at 2 institutions in 1 country.

Lindsey S MarmontDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115.ORCID 0000-0002-4225-2690
Thomas G BernhardtDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115; thomas_bernhardt@hms.harvard.edu.
Harvard University · USHoward Hughes Medical Institute · US

Funding

Peptidoglycan Biogenesis in Escherichia ColiR01AI083365 · NIAID · HARVARD MEDICAL SCHOOL · PI Thomas G Bernhardt · 2010 to 2026
$8.3M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI083365
6 · The paper itself

Abstract

Cell division in bacteria is mediated by a multiprotein assembly called the divisome. A major function of this machinery is the synthesis of the peptidoglycan (PG) cell wall that caps the daughter poles and prevents osmotic lysis of the newborn cells. Recent studies have implicated a complex of FtsW and FtsI (FtsWI) as the essential PG synthase within the divisome; however, how PG polymerization by this synthase is regulated and coordinated with other activities within the machinery is not well understood. Previous results have implicated a conserved subcomplex of division proteins composed of FtsQ, FtsL, and FtsB (FtsQLB) in the regulation of FtsWI, but whether these proteins act directly as positive or negative regulators of the synthase has been unclear. To address this question, we purified a five-member

Indexed as

Bacterial ProteinsCell Cycle ProteinsCell WallMembrane ProteinsCytokinesisEscherichia coliPseudomonas aeruginosaBacterial ProteinsCell Cycle ProteinsFtsX protein, bacteriaMembrane Proteinscell divisioncell walldivisomepeptidoglycanseptal ring

Identifiers

PMID32907942
PMCPMC7519343
OpenAlexW3084307332

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.