ReviewmicroLife2023
The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.
Review in microLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 13 citations in OpenAlex.
- Differences in β-lactamase activity and carbapenem resistance among theAntimicrobial agents and chemotherapy · 2026Article
- From Host-Derived Pressures to the Environmental Anti-Antimicrobial Peptides Resistome: Mechanisms, Reservoirs and Implications for Therapeutic Peptide Design.Marine drugs · 2026Review
- Comparative Transcriptomic Analyses Reveal Potential Stp1 Regulatory Roles Independent of Sre1 inInternational journal of molecular sciences · 2025Article
- Characterization of two orthologs of bacterial intramembrane metalloprotease RseP by native mass spectrometry.Analytical and bioanalytical chemistry · 2025Article
- Inhibitory proteins ofJournal of bacteriology · 2025Article
- Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state.Science advances · 2025Article
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- Substrate engagement by the intramembrane metalloprotease SpoIVFB.Nature communications · 2024Article
- The Impact ofPathogens (Basel, Switzerland) · 2024Review
- Revisiting the Multifaceted Roles of Bacteriocins : The Multifaceted Roles of Bacteriocins.Microbial ecology · 2024Review
- Lactiplantibacillus plantarum as a novel platform for production and purification of integral membrane proteins using RseP as the benchmark.Scientific reports · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-2-proteases are a class of intramembrane proteases involved in regulated intramembrane proteolysis. Regulated intramembrane proteolysis is a highly conserved signaling mechanism that commonly involves sequential digestion of an anti-sigma factor by a site-1- and site-2-protease in response to external stimuli, resulting in an adaptive transcriptional response. Variation of this signaling cascade continues to emerge as the role of site-2-proteases in bacteria continues to be explored. Site-2-proteases are highly conserved among bacteria and play a key role in multiple processes, including iron uptake, stress response, and pheromone production. Additionally, an increasing number of site-2-proteases have been found to play a pivotal role in the virulence properties of multiple human pathogens, such as alginate production in
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.