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

Critical role of a ferritin-like protein in the control of Listeria monocytogenes cell envelope structure and stability under β-lactam pressure.

PloS one - 1 Jan 2013

Krawczyk-Balska Agata, Lipiak Magdalena

Abstract excerpt

The human pathogen Listeria monocytogenes is susceptible to the β-lactam antibiotics penicillin G and ampicillin, and these are the drugs of choice for the treatment of listerial infections. However, these antibiotics exert only a bacteriostatic effect on this bacterium and consequently, L. monocytogenes is regarded as β-lactam tolerant. It is widely accepted that the phenomenon of bacterial tolerance to...

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 Cell Wall
Share to Chromatography, High Pressure Liquid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ferritins

Share to Listeria monocytogenes

Share to Peptide Fragments

Share to Peptidoglycan

Share to Teichoic Acids

Source

Open in PubMed Open full text

Identifiers

PMID: 24204978
DOI: 10.1371/journal.pone.0077808
PMCID: PMC3812014

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Critical role of a ferritin-like protein in the control of Listeria monocytogenes cell envelope structure and stability under β-lactam pressure.PMID 24204978Read ↗

Comprehensive proteomic analysis and pathogenic role of membrane vesicles of Listeria monocytogenes serotype 4b reveals proteins associated with virulence and their possible interaction with hostSemantic proximity Read ↗

Fatty acids regulate stress resistance and virulence factor production for Listeria monocytogenes.Semantic proximity Read ↗

Recent advances in understanding Listeria monocytogenes infection: the importance of subcellular and physiological contextSemantic proximity Read ↗

The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells.Semantic proximity Read ↗

Universal stress proteins are important for oxidative and acid stress resistance and growth of Listeria monocytogenes EGD-e in vitro and in vivo.Semantic proximity Read ↗

Contribution of the multiple Type I signal peptidases to the secretome of Listeria monocytogenes: deciphering their specificity for secreted exoproteins by exoproteomic analysis.Semantic proximity Read ↗

Fine-tuning of outer membrane–peptidoglycan tethering by the redox-active lipoprotein LppB from Salmonella entericaSemantic proximity Read ↗

Lactoferrin impairs pathogen virulence through its proteolytic activitySemantic proximity Read ↗

Plasticity of listeriolysin O pores and its regulation by pH and unique histidine [corrected].Semantic proximity Read ↗

A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity.Semantic proximity Read ↗

A novel mutation within the central Listeria monocytogenes regulator PrfA that results in constitutive expression of virulence gene products.Semantic proximity Read ↗

The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells.Semantic proximity Read ↗

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