Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Colicins, spermine and cephalosporins: a competitive interaction with the OmpF eyelet.

The Biochemical journal - 15 Nov 2003

Bredin Jérôme, Simonet Valérie, Iyer Ramkumar, Delcour Anne H, Pagès Jean-Marie

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding, Competitive
Share to Biological Transport
Share to Cephalosporins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Colicins

Share to Drug Resistance, Bacterial

Share to Porins

Share to Spermine

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 12882645
DOI: 10.1042/BJ20030814
PMCID: PMC1223742

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Colicins, spermine and cephalosporins: a competitive interaction with the OmpF eyelet.PMID 12882645Read ↗

Beta-lactam screening by specific residues of the OmpF eyelet.Semantic proximity Read ↗

Site-directed mutagenesis studies to probe the role of specific residues in the external loop (L3) of OmpF and OmpC porins in susceptibility of Serratia marcescens to antibiotics.Semantic proximity Read ↗

Mutations in a Conserved Domain of E. coli MscS to the Most Conserved Superfamily Residue Leads to Kinetic Changes.Semantic proximity Read ↗

Phenotypic characterization of pore mutants of the Vibrio cholerae porin OmpU.Semantic proximity Read ↗

Combinatorial mutagenesis analysis of residues in the channel constriction loop L3 and neighbouring beta-strands in the LamB glycoporin of Escherichia coli.Semantic proximity Read ↗

Analysis of the G93E mutant allele of KpsM, the membrane component of an ABC transporter involved in polysialic acid translocation in Escherichia coli K1.Semantic proximity Read ↗

Cadaverine inhibition of porin plays a role in cell survival at acidic pH.Semantic proximity Read ↗

Structure, Function and Regulation of Outer Membrane Proteins Involved in Drug Transport in Enterobactericeae: the OmpF/C – TolC CaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.