ArticlemBio2021
Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.
Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Traditional plant urologicals curb early uropathogenic E. coli infection and strengthen host innate defense.Applied microbiology and biotechnology · 2026Article
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- Surfing in the storm: how Paraburkholderia xenovorans thrives under stress during biodegradation of toxic aromatic compounds and other stressors.FEMS microbiology reviews · 2025Review
- Article
- Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.Annual review of microbiology · 2024Review
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Genomic mining of Vibrio parahaemolyticus highlights prevalence of antimicrobial resistance genes and new genetic markers associated with AHPND and tdh + /trh + genotypes.BMC genomics · 2024Article
- A hydrophilic polyimidazolium antibiotic targeting the membranes of Gram-negative bacteria.The Journal of antimicrobial chemotherapy · 2023Article
- Modulation ofBiomedicines · 2023Article
- FkpA enhances membrane protein folding using an extensive interaction surface.Protein science : a publication of the Protein Society · 2023Article
- Article
- CRISPRactivation-SMS, a message for PAM sequence independent gene up-regulation in Escherichia coli.Nucleic acids research · 2022Article
- Effects of Cinnamon Essential Oil on Oxidative Damage and Outer Membrane Protein Genes ofFoods (Basel, Switzerland) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gram-negative bacteria have a multicomponent and constitutively active periplasmic chaperone system to ensure the quality control of their outer membrane proteins (OMPs). Recently, OMPs have been identified as a new class of vulnerable targets for antibiotic development, and therefore a comprehensive understanding of OMP quality control network components will be critical for discovering antimicrobials. Here, we demonstrate that the periplasmic chaperone Spy protects certain OMPs against protein-unfolding stress and can functionally compensate for other periplasmic chaperones, namely Skp and FkpA, in the Escherichia coli K-12 MG1655 strain. After extensive
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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.