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

Involvement of mutation in ampD I, mrcA, and at least one additional gene in β-lactamase hyperproduction in Stenotrophomonas maltophilia.

Antimicrobial agents and chemotherapy - 1 Nov 2013

Talfan Asmaa, Mounsey Oliver, Charman Matthew, Townsend Eleanor, Avison Matthew B

Abstract excerpt

It has been reported that targeted disruption of ampD I or mrcA causes β-lactamase hyperproduction in Stenotrophomonas maltophilia. We show here that β-lactamase-hyperproducing laboratory selected mutants and clinical isolates can have wild-type ampD I and mrcA genes, implicating mutation of at least one additional gene in this phenotype. The involvement of mutations at multiple loci in the activation of...

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 Escherichia coli

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

Share to Gene Expression Regulation, Bacterial

Share to Genetic Complementation Test

Share to N-Acetylmuramoyl-L-alanine Amidase

Share to Peptidoglycan

Share to Proteolysis

Share to Stenotrophomonas maltophilia

Source

Open in PubMed Open full text

Identifiers

PMID: 23979761
DOI: 10.1128/AAC.01446-13
PMCID: PMC3811264

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

Involvement of mutation in ampD I, mrcA, and at least one additional gene in β-lactamase hyperproduction in Stenotrophomonas maltophilia.PMID 23979761Read ↗

Inactivation of mrcA gene derepresses the basal-level expression of L1 and L2 β-lactamases in Stenotrophomonas maltophilia.Semantic proximity Read ↗

TonB dependent uptake of β-lactam antibiotics in the opportunistic human pathogen <i>Stenotrophomonas maltophilia</i>Semantic proximity Read ↗

Cell Wall Recycling-Linked Coregulation of AmpC and PenB β-Lactamases through ampD Mutations in Burkholderia cenocepacia.Semantic proximity Read ↗

Induction of L1 and L2 beta-lactamase production in Stenotrophomonas maltophilia is dependent on an AmpR-type regulator.Semantic proximity Read ↗

A LacI-family regulator activates maltodextrin metabolism of Enterococcus faecium.Semantic proximity Read ↗

TonB-dependent uptake of β-lactam antibiotics in the opportunistic human pathogen Stenotrophomonas maltophilia.Semantic proximity Read ↗

NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophilia.Semantic proximity Read ↗

Novel mechanisms of efflux-mediated levofloxacin resistance and reduced amikacin susceptibility in <i>Stenotrophomonas maltophilia</i>Semantic proximity Read ↗

AmpN-AmpG operon is essential for expression of L1 and L2 beta-lactamases in Stenotrophomonas maltophilia.Semantic proximity Read ↗

ampR gene mutations that greatly increase class C beta-lactamase activity in Enterobacter cloacae.Semantic proximity Read ↗

Mutations in Ribosomal Protein RplA or Treatment with Ribosomal Acting Antibiotics Activates Production of Aminoglycoside Efflux Pump SmeYZ in Stenotrophomonas maltophilia.Semantic proximity Read ↗

Differential regulation of L1 and L2 beta-lactamase expression in Stenotrophomonas maltophilia.Semantic proximity Read ↗

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