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

H-NS modulates multidrug resistance of Salmonella enterica serovar Typhimurium by repressing multidrug efflux genes acrEF.

Antimicrobial agents and chemotherapy - 1 Aug 2009

Nishino Kunihiko, Hayashi-Nishino Mitsuko, Yamaguchi Akihito

Abstract excerpt

Screening of Salmonella mutants for the ability to increase beta-lactam resistance has led to the identification of a mutation in hns, which codes for the histone-like nucleoid structuring protein (H-NS). In this study, we report that H-NS modulates multidrug resistance through repression of the genes that encode the AcrEF multidrug efflux pump in Salmonella enterica serovar Typhimurium.

Read the complete abstract on PubMed

Topics

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

Share to Anti-Bacterial Agents
Share to beta-Lactams
Share to Drug Resistance, Multiple, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Membrane Transport Proteins

Share to Microbial Sensitivity Tests

Share to Salmonella typhimurium

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 19506059
DOI: 10.1128/AAC.00371-09
PMCID: PMC2715579

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

H-NS modulates multidrug resistance of Salmonella enterica serovar Typhimurium by repressing multidrug efflux genes acrEF.PMID 19506059Read ↗

Histone-like nucleoid-structuring protein (H-NS) regulatory role in antibiotic resistance in Acinetobacter baumannii.Semantic proximity Read ↗

Histone-like Nucleoid-structuring Protein (H-NS) Regulatory Role in Antibiotic Resistance in Acinetobacter BaumanniiSemantic proximity Read ↗

Expression and mutational analysis of the nucleoid-associated protein H-NS of Salmonella typhimurium.Semantic proximity Read ↗

RNA-seq analysis identifies new genes regulated by the histone-like nucleoid structuring protein (H-NS) affecting Vibrio cholerae virulence, stress response and chemotaxis.Semantic proximity Read ↗

Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella.Semantic proximity Read ↗

Perturbing H-NS function reveals roles in restricting virulence heterogeneity and pathogen adaptation.Semantic proximity Read ↗

H-NS plays a role in expression of Acinetobacter baumannii virulence features.Semantic proximity Read ↗

Long-Distance Effects of H-NS Binding in the Control of hilD Expression in the Salmonella SPI1 LocusSemantic proximity Read ↗

The chromatin-associated protein H-NS.Semantic proximity Read ↗

Silencing by H-NS potentiated the evolution of Salmonella.Semantic proximity Read ↗

Integration host factor alleviates H-NS silencing of the Salmonella enterica serovar Typhimurium master regulator of SPI1, hilA.Semantic proximity Read ↗

The small nucleoid-binding proteins H-NS, HU, and Fis affect hilA expression in Salmonella enterica serovar Typhimurium.Semantic proximity Read ↗

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