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

Crystal Structures of the Apo and Penicillin-acylated Forms of the BlaR1 β-Lactam Sensor of Staphylococcus aureus

19 Aug 2004

Abstract excerpt

Staphylococcus aureus is among the most prevalent and antibiotic-resistant of pathogenic bacteria. The resistance of S. aureus to prototypal beta-lactam antibiotics is conferred by two mechanisms: (i) secretion of hydrolytic beta-lactamase enzymes and (ii) production of beta-lactam-insensitive penicillin-binding proteins (PBP2a). Despite their distinct modes of resistance, expression of these proteins is...

Read the complete abstract on PubMed

Topics

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

Share to Antibiotic Resistance in Bacteria
Share to Antimicrobial Resistance in Staphylococcus
Share to Bacterial biofilms and quorum sensing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15322076
DOI: 10.1074/jbc.m407054200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal Structures of the Apo and Penicillin-acylated Forms of the BlaR1 β-Lactam Sensor of Staphylococcus aureusPMID 15322076Read ↗

Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureusSemantic proximity Read ↗

Mechanisms of Methicillin Resistance in <i>Staphylococcus aureus</i>Semantic proximity Read ↗

The Anti-Repressor MecR2 Promotes the Proteolysis of the mecA Repressor and Enables Optimal Expression of β-lactam Resistance in MRSASemantic proximity Read ↗

On the transcriptional regulation of methicillin resistance: MecI repressor in complex with its operator.Semantic proximity Read ↗

Structural analysis of the antibiotic-recognition mechanism of MarR proteinsSemantic proximity Read ↗

How allosteric control of Staphylococcus aureus penicillin binding protein 2a enables methicillin resistance and physiological functionSemantic proximity Read ↗

Structural and kinetic analysis of the monofunctional Staphylococcus aureus PBP1Semantic proximity Read ↗

Redefining the role of the β-lactamase locus in methicillin-resistant Staphylococcus aureus: β-lactamase regulators disrupt the MecI-mediated strong repression on mecA and optimize the phenotypic expression of resistance in strains with constitutive mecA expression.Semantic proximity Read ↗

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

Novel mutations in penicillin-binding protein genes in clinical Staphylococcus aureus isolates that are methicillin resistant on susceptibility testing, but lack the mec geneSemantic proximity Read ↗

Activation of the Extracytoplasmic Function σ factor σ <sup>P</sup> by β-lactams in <i>Bacillus thuringiensis</i> requires the site-2 protease RasPSemantic proximity Read ↗

Distinctive Attributes of β-Lactam Target Proteins in <i>Acinetobacter baumannii</i> Relevant to Development of New AntibioticsSemantic proximity Read ↗

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