ArticleThe Biochemical journal2003
Colicins, spermine and cephalosporins: a competitive interaction with the OmpF eyelet.
Article in The Biochemical journal, 2003. 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.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- The binding of antibiotics in OmpF porin.Structure (London, England : 1993) · 2013Article
- Implication of porins in beta-lactam resistance of Providencia stuartii.The Journal of biological chemistry · 2010Article
- Unimolecular study of the interaction between the outer membrane protein OmpF from E. coli and an analogue of the HP(2-20) antimicrobial peptide.Journal of bioenergetics and biomembranes · 2010Article
- Cation-selective pathway of OmpF porin revealed by anomalous X-ray diffraction.Journal of molecular biology · 2010Article
- Crystal structures of the OmpF porin: function in a colicin translocon.The EMBO journal · 2008Article
- Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU.Journal of bacteriology · 2007Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import.Biophysical journal · 2004Article
- Physiological polyamines: simple primordial stress molecules.Journal of cellular and molecular medicineReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The L3 loop is an important feature of the OmpF porin structure, contributing to both channel size and electrostatic properties. Colicins A and N, spermine, and antibiotics that use OmpF to penetrate the cell, were used to investigate the structure-function relationships of L3. Spermine was found to protect efficiently cells expressing wild-type OmpF from colicin action. Among other solutes, sugars had minor effects on colicin A activity, whereas competitions between colicin A and antibiotic fluxes were observed. Among the antibiotics tested, cefepime appeared the most efficient. Escherichia coli cells expressing various OmpF proteins mutated in the eyelet were tested for their susceptibility to colicin A, and resistant strains were found only among L3 mutants. Mutations at residues 119 and 120 were the most effective at conferring resistance to colicin A, probably due to epitope structure alteration, as revealed by a specific antipeptide. More detailed information was obtained on mutants D113A and D121A, by focusing on the kinetics of colicin A and colicin N activities through measurements of potassium efflux. D113 appeared to play an essential role for colicin A activity, whereas colicin N activity was more dependent on D121 than on D113.
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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.