ArticleProceedings of the National Academy of Sciences of the United States of America2025
Versatile NTP recognition and domain fusions expand the functional repertoire of the ParB-CTPase fold beyond chromosome segregation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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
5 citing papers in PubMed.
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Plasmid-encoded host reprogramming promotes plasmid dissemination.bioRxiv : the preprint server for biology · 2026Article
- Stable inheritance of the Streptomyces linear plasmid SCP1 by dual ParABS partition systems.Nucleic acids research · 2026Article
- Uncovering ParB-dependent and -independent subclasses of T-dioxygenases from bacteriophage.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The role of the VirB ligand CTP in the molecular mechanism of transcriptional anti-silencing in Shigella flexneri.Nucleic acids research · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Nucleotide triphosphate (NTP)-dependent molecular switches regulate essential cellular processes by cycling between active and inactive states through nucleotide binding and hydrolysis. These mechanisms were long thought to rely exclusively on ATPase or GTPase proteins, until the discovery of CTPase activity in the bacterial chromosome segregation protein ParB. In the ParAB
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Registered trials
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