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

Role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins in AmpC expression, β-lactam resistance, and peptidoglycan structure.

Antimicrobial agents and chemotherapy - 1 Jul 2015

Ropy Alaa, Cabot Gabriel, Sánchez-Diener Irina, Aguilera Cristian, Moya Bartolome, Ayala Juan A, Oliver Antonio

Abstract excerpt

This study aimed to characterize the role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins (LMM PBPs), namely, PBP4 (DacB), PBP5 (DacC), and PBP7 (PbpG), in peptidoglycan composition, β-lactam resistance, and ampC regulation. For this purpose, we constructed all single and multiple mutants of dacB, dacC, pbpG, and ampC from the wild-type P. aeruginosa PAO1 strain. Peptidoglycan composition...

Read the complete abstract on PubMed

Topics

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

Share to beta-Lactam Resistance
Share to beta-Lactams

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Boron Compounds

Share to Carboxypeptidases

Share to Gene Knockout Techniques

Share to Penicillin-Binding Proteins

Share to Penicillins

Share to Peptidoglycan

Source

Open in PubMed Open full text

Identifiers

PMID: 25896695
DOI: 10.1128/AAC.05150-14
PMCID: PMC4468666

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins in AmpC expression, β-lactam resistance, and peptidoglycan structure.PMID 25896695Read ↗

Structural Analysis of the Role of Pseudomonas aeruginosa Penicillin-Binding Protein 5 in β-Lactam ResistanceSemantic proximity Read ↗

A potential space-making role in cell wall biogenesis for SltB1and DacB revealed by a beta-lactamase induction phenotype in Pseudomonas aeruginosa.Semantic proximity Read ↗

Pan-β-Lactam Resistance Development in Pseudomonas aeruginosa Clinical Strains: Molecular Mechanisms, Penicillin-Binding Protein Profiles, and Binding AffinitiesSemantic proximity Read ↗

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

Conserved mechanism of cell-wall synthase regulation revealed by the identification of a new PBP activator in Pseudomonas aeruginosa.Semantic proximity Read ↗

A putative low-molecular-mass penicillin-binding protein (PBP) of Mycobacterium smegmatis exhibits prominent physiological characteristics of DD-carboxypeptidase and beta-lactamase.Semantic proximity Read ↗

An Update on the Role of Penicillin Binding Protein-4 (PBP4) in β-Lactam Resistance of <em>Staphylococcus aureus</em>Semantic proximity Read ↗

Complex Regulation Pathways of AmpC-Mediated β-Lactam Resistance in Enterobacter cloacae Complex.Semantic proximity Read ↗

Pseudomonas aeruginosa Alters Peptidoglycan Composition under Nutrient Conditions Resembling Cystic Fibrosis Lung InfectionsSemantic proximity Read ↗

Structural and Regulatory Changes in PBP4 Trigger Decreased β-Lactam Susceptibility in Enterococcus faecalisSemantic proximity Read ↗

PBP5, PBP6 and DacD play different roles in intrinsic β-lactam resistance of Escherichia coli.Semantic proximity Read ↗

Functional and structural analyses of amino acid sequence variation in PDC β-lactamase reveal different mechanistic pathways toward cefiderocol resistance in Pseudomonas aeruginosaSemantic proximity Read ↗

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