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

Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.

PloS one - 1 Jan 2012

Sarkar Sujoy K, Dutta Mouparna, Kumar Akash, Mallik Dhriti, Ghosh Anindya S

Abstract excerpt

The combination of antibiotics is one of the strategies to combat drug-resistant bacteria, though only a handful of such combinations are in use, such as the β-lactam combinations. In the present study, the efficacy of a specific sub-inhibitory concentration of cefsulodin with other β-lactams was evaluated against a range of Gram-negative clinical isolates. This approach increased the sensitivity of the isolates,...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactamases
Share to Drug Evaluation, Preclinical
Share to Drug Resistance, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Fluorescence

Share to Microbial Sensitivity Tests

Share to O Antigens

Share to Penicillin-Binding Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23139798
DOI: 10.1371/journal.pone.0048598
PMCID: PMC3490869

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 · 12 closest

Sub-inhibitory cefsulodin sensitization of E. coli to β-lactams is mediated by PBP1b inhibition.PMID 23139798Read ↗

Tackling the Antibiotic Resistance Caused by Class A β-Lactamases through the Use of β-Lactamase Inhibitory ProteinSemantic proximity Read ↗

Penicillin-binding proteins and beta-lactam resistance.Semantic proximity Read ↗

PBP4: A New Perspective on Staphylococcus aureus β-Lactam ResistanceSemantic proximity Read ↗

New β-lactam antibiotics and β-lactamase inhibitorsSemantic proximity Read ↗

Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.Semantic proximity Read ↗

Classification of group B streptococci with reduced β-lactam susceptibility (GBS-RBS) based on the amino acid substitutions in PBPsSemantic proximity Read ↗

Impact of transferable β-lactamases and intrinsic AmpC amino acid substitutions on the activity of cefiderocol against wild-type and iron uptake-deficient mutants of Pseudomonas aeruginosaSemantic proximity Read ↗

Altered PBP4 and GdpP functions synergistically mediate MRSA-like high-level, broad-spectrum β-lactam resistance in Staphylococcus aureus.Semantic proximity Read ↗

Clinically Relevant Gram-Negative Resistance Mechanisms Have No Effect on the Efficacy of MC-1, a Novel Siderophore-Conjugated MonocarbamSemantic proximity Read ↗

Correlation between penicillin-binding protein 2 mutations and carbapenem resistance in Escherichia coli.Semantic proximity Read ↗

Frameshift Mutations in Genes Encoding PBP3 and PBP4 Trigger an Unusual, Extreme β-Lactam Resistance Phenotype in Burkholderia multivorans.Semantic proximity Read ↗

Investigation of cross-opsonic effect leads to the discovery of PPIase- domain containing protein vaccine target to prevent infections by Gram-positive ESKAPE pathogensSemantic proximity Read ↗

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