ArticleeLife2021
The Lon protease temporally restricts polar cell differentiation events during the
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 22 citations in OpenAlex.
- Lon protease reprograms cellular physiology ofFrontiers in microbiology · 2026Article
- Direct and indirect pathways linking the Lon protease to motility behaviors in the pathogen Pseudomonas aeruginosa.PLoS pathogens · 2025Article
- Article
- Allosteric modulation of the Lon protease by effector binding and local charges.bioRxiv : the preprint server for biology · 2024Article
- Proteolytic control of FixT by the Lon protease impacts FixLJ signaling inJournal of bacteriology · 2024Article
- The heat shock protein LarA activates the Lon protease in response to proteotoxic stress.Nature communications · 2023Article
- Regulation of the general stress response sigma factor σJournal of bacteriology · 2023Article
- Targeting bacterial degradation machinery as an antibacterial strategy.The Biochemical journal · 2023Review
- Cell cycle-dependent organization of a bacterial centromere through multi-layered regulation of the ParABS system.PLoS genetics · 2023Article
- Proteolysis dependent cell cycle regulation in Caulobacter crescentus.Cell division · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The highly conserved protease Lon has important regulatory and protein quality control functions in cells from the three domains of life. Despite many years of research on Lon, only a few specific protein substrates are known in most organisms. Here, we used a quantitative proteomics approach to identify novel substrates of Lon in the dimorphic bacterium
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.