ArticleJournal of bacteriology2002
Identification of a protein that inactivates the competence-stimulating peptide of Streptococcus pneumoniae.
Article in Journal of bacteriology, 2002. 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.
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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.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Identification and Characterization of Negative Regulators of Rgg1518 Quorum Sensing in Streptococcus pneumoniae.Journal of bacteriology · 2023Article
- Intensive targeting of regulatory competence genes by transposable elements in streptococci.Molecular genetics and genomics : MGG · 2019Article
- Streptococcus endopeptidases promote HPV infection in vitro.MicrobiologyOpen · 2019Article
- Transcriptome analysis of Streptococcus pneumoniae treated with the designed antimicrobial peptides, DM3.Scientific reports · 2016Article
- Oscillations in continuous culture populations of Streptococcus pneumoniae: population dynamics and the evolution of clonal suicide.Proceedings. Biological sciences · 2009Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Competence for genetic transformation of Streptococcus pneumoniae is a transient physiological property inducible by a competence-stimulating peptide (CSP). A 68-kDa CSP-inactivating protein was previously obtained following lithium chloride (LiCl) extraction. By the same protocol, a CSP-inactivating protein was purified and identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry as an endopeptidase, PepO. Analysis of a pepO mutant provided no support for the hypothesis that PepO participates in competence regulation. To reconcile in vitro and in vivo data, we suggest that LiCl treatment results in the release of intracellular molecules, including PepO.
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Registered trials
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