ReviewTrends in microbiology2017
Protecting from Envelope Stress: Variations on the Phage-Shock-Protein Theme.
Review in Trends in microbiology, 2017. 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 38 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
38 citing papers in PubMed, 68 citations in OpenAlex.
- The phage shock protein A (PspA) maintains membrane potential and supports NADH dehydrogenase function in mycobacteria.bioRxiv : the preprint server for biology · 2026Article
- Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026Review
- The phage shock protein response of Listeria monocytogenes influences tolerance to the multipeptide bacteriocin garvicin KS.Applied microbiology and biotechnology · 2026Article
- Membrane binding of a cyanobacterial ESCRT-III protein crucially involves the helix α1-3 hairpin conserved in all superfamily members.Protein science : a publication of the Protein Society · 2025Article
- BacterialBiosensors · 2025Article
- The bacterial ESCRT-III PspA rods thin lipid tubules and increase membrane curvature through helix α0 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.Nature structural & molecular biology · 2025Article
- Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.Protein science : a publication of the Protein Society · 2024Article
- The phage shock protein (PSP) envelope stress response: discovery of novel partners and evolutionary history.mSystems · 2024Article
- The metabolic slowdown caused by the deletion ofAntimicrobial agents and chemotherapy · 2024Article
- Boosting Fitness Costs Associated with Antibiotic Resistance in the Gut: On the Way to Biorestoration of Susceptible Populations.Biomolecules · 2024Review
- Structure of the SigE regulatory network inFrontiers in microbiology · 2024Article
- The LiaFSR-LiaX System Mediates Resistance of Enterococcus faecium to Peptide Antibiotics and to Aureocin A53- and Enterocin L50-Like Bacteriocins.Microbiology spectrum · 2023Article
- Inference of transcriptome signatures of Escherichia coli in long-term stationary phase.Scientific reports · 2023Article
- Cyanobacterial membrane dynamics in the light of eukaryotic principles.Bioscience reports · 2023Article
- SigE: A master regulator ofFrontiers in microbiology · 2023Review
- Emerging Research Topics in the Vibrionaceae and the Squid-Microorganisms · 2022Review
- Phyletic Distribution and Diversification of the Phage Shock Protein Stress Response System in Bacteria and Archaea.mSystems · 2022Article
- Isolation of Persister Cells ofInternational journal of molecular sciences · 2021Article
- Active maintenance of proton motive force mediates starvation-induced bacterial antibiotic tolerance in Escherichia coli.Communications biology · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
During envelope stress, critical inner-membrane functions are preserved by the phage-shock-protein (Psp) system, a stress response that emerged from work with Escherichia coli and other Gram-negative bacteria. Reciprocal regulatory interactions and multiple effector functions are well documented in these organisms. Searches for the Psp system across phyla reveal conservation of only one protein, PspA. However, examination of Firmicutes and Actinobacteria reveals that PspA orthologs associate with non-orthologous regulatory and effector proteins retaining functions similar to those in Gram-negative counterparts. Conservation across phyla emphasizes the long-standing importance of the Psp system in prokaryotes, while inter- and intra-phyla variations within the system indicate adaptation to different cell envelope structures, bacterial lifestyles, and/or bacterial morphogenetic strategies.
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.