Evidence map›Paper›PMID 27039284›Full record

ArticleMicrobiologyOpen2016

Molecular and proteome analyses highlight the importance of the Cpx envelope stress system for acid stress and cell wall stability in Escherichia coli.

Kristin Surmann, Emina Ćudić, Elke Hammer, Sabine Hunke

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Cpx-signalling innpj antimicrobials and resistance · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Kristin SurmannDepartment of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, University Medicine Greifswald, Friedrich-Ludwig-Jahn-Straße 15A, Greifswald, 17475, Germany.
Emina ĆudićFB 5 Microbiology, Department of Biology/Chemistry, University Osnabrück, Barbarastraße 11, Osnabrück, 49076,, Germany.
Elke HammerDepartment of Functional Genomics, Interfaculty Institute of Genetics and Functional Genomics, University Medicine Greifswald, Friedrich-Ludwig-Jahn-Straße 15A, Greifswald, 17475, Germany.
Sabine HunkeFB 5 Microbiology, Department of Biology/Chemistry, University Osnabrück, Barbarastraße 11, Osnabrück, 49076,, Germany.
Osnabrück University · DEUniversitätsmedizin Greifswald · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two-component systems (TCS) play a pivotal role for bacteria in stress regulation and adaptation. However, it is not well understood how these systems are modulated to meet bacterial demands. Especially, for those TCS using an accessory protein to integrate additional signals, no data concerning the role of the accessory proteins within the coordination of the response is available. The Cpx envelope stress two-component system, composed of the sensor kinase CpxA and the response regulator CpxR, is orchestrated by the periplasmic protein CpxP which detects misfolded envelope proteins and inhibits the Cpx system in unstressed cells. Using selected reaction monitoring, we observed that the amount of CpxA and CpxR, as well as their stoichiometry, are only marginally affected, but that a 10-fold excess of CpxP over CpxA is needed to switch off the Cpx system. Moreover, the relative quantification of the proteome identified not only acid stress response as a new indirect target of the Cpx system, but also suggests a general function of the Cpx system for cell wall stability.

Indexed as

Adaptation, PhysiologicalBacterial ProteinsCell WallEscherichia coliEscherichia coli ProteinsMass SpectrometryMembrane ProteinsProtein KinasesProteomeProteomicsStress, PhysiologicalTranscription FactorsBacterial ProteinsCpxA protein, E coliCpxP protein, E coliCpxR protein, BacteriaEscherichia coli ProteinsMembrane ProteinsProtein KinasesProteomeRseA protein, E coliTranscription FactorsCpx RAP systemEscherichia coliproteome profileSRMtwo-component system.

Identifiers

PMID27039284
PMCPMC4985592
OpenAlexW2326944537

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.