ArticlemBio2019
Checks and Balances in Bacterial Cell Division.
Article in mBio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- In Silico Druggability Assessment ofAntibiotics (Basel, Switzerland) · 2026Article
- Deciphering the molecular mechanism of the bacterial division motor TolQRA.Cell discovery · 2025Article
- Article
- Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome.Nature communications · 2023Article
- Peptide-based covalent inhibitors of protein-protein interactions.Journal of peptide science : an official publication of the European Peptide Society · 2023Review
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- OmpR and Prc contribute to switch the Salmonella morphogenetic program in response to phagosome cues.Molecular microbiology · 2022Article
- Covalent Proteomimetic Inhibitor of the Bacterial FtsQB Divisome Complex.Journal of the American Chemical Society · 2022Article
- Early midcell localization of Escherichia coli PBP4 supports the function of peptidoglycan amidases.PLoS genetics · 2022Article
- How Does the Spatial Confinement of FtsZ to a Membrane Surface Affect Its Polymerization Properties and Function?Frontiers in microbiology · 2022Review
- Cinnamaldehyde derivatives act as antimicrobial agents againstFrontiers in microbiology · 2022Article
- A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- Engineering spatiotemporal organization and dynamics in synthetic cells.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2021Review
- Peptidoglycan: Structure, Synthesis, and Regulation.EcoSal Plus · 2021Article
- The bacterial cell division protein fragmentThe Journal of biological chemistry · 2020Article
- Bacteriophage SP01 Gene Product 56 Inhibits Bacillus subtilis Cell Division by Interacting with FtsL and Disrupting Pbp2B and FtsW Recruitment.Journal of bacteriology · 2020Article
- MreC and MreD balance the interaction between the elongasome proteins PBP2 and RodA.PLoS genetics · 2020Article
- Article
- SosA inhibits cell division in Staphylococcus aureus in response to DNA damage.Molecular microbiology · 2019Article
- The Cell Wall Hydrolytic NlpC/P60 Endopeptidases in Mycobacterial Cytokinesis: A Structural Perspective.Cells · 2019Review
Corrections and comments
- Comment on
- Erratum issued
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of the division machinery in Gram-negative and Gram-positive bacteria occurs in two time-dependent steps. First, the FtsZ proto-ring localizes at midcell including some FtsN molecules. Subsequently, the proteins that catalyze and regulate septal peptidoglycan (PG) synthesis are recruited including among others, the FtsBLQ-PB1B-FtsW-PBP3 complex. Further accumulation of FtsN finally allows initiation of cell division. It was known that FtsA and FtsQLB somehow prevented this initiation. Recently, A. Boes, S. Olatunji, E. Breukink, and M. Terrak (mBio 10:e01912-18, 2019, https://doi.org/10.1128/mBio.01912-18) reported that this is caused by inhibition of the activity of the PG synthases by FtsBLQ, which has to be outcompeted by accumulation of the PBP1b activating FtsN. This supports a central structural as well as regulatory role for the FtsBLQ protein complex that is conserved only in prokaryotes, making it an attractive target for antibiotic development.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.