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

Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.

Antimicrobial agents and chemotherapy - 1 Nov 2015

Patel Meha P, Fryszczyn Bartlomiej G, Palzkill Timothy

Abstract excerpt

The widespread use of oxyimino-cephalosporin antibiotics drives the evolution of the CTX-M family of β-lactamases that hydrolyze these drugs and confer antibiotic resistance. Clinically isolated CTX-M enzymes carrying the P167S or D240G active site-associated adaptive mutation have a broadened substrate profile that includes the oxyimino-cephalosporin antibiotic ceftazidime. The D240G substitution is known to...

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-Lactamases

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

Share to Ceftazidime

Share to Drug Resistance, Bacterial

Share to Escherichia coli

Share to Evolution, Molecular

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 26282414
DOI: 10.1128/AAC.00618-15
PMCID: PMC4604362

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

Characterization of the global stabilizing substitution A77V and its role in the evolution of CTX-M β-lactamases.PMID 26282414Read ↗

SHV-129: A Gateway to Global Suppressors in the SHV β-Lactamase Family?Semantic proximity Read ↗

Stabilizing Mutations Enhance Evolvability of BlaC β-lactamase by Widening the Mutational Landscape.Semantic proximity Read ↗

Distant and new mutations in CTX-M-1 beta-lactamase affect cefotaxime hydrolysis.Semantic proximity Read ↗

Mutation of the conserved Asp-Asp pair impairs the structure, function, and inhibition of CTX-M Class A β-lactamase.Semantic proximity Read ↗

Detailed investigation of catalytically important residues of class A β-lactamaseSemantic proximity Read ↗

A triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysis.Semantic proximity Read ↗

Unveiling the evolution routes of TEM-type extended-spectrum β-lactamases.Semantic proximity Read ↗

Roles of residues Cys69, Asn104, Phe160, Gly232, Ser237, and Asp240 in extended-spectrum beta-lactamase Toho-1.Semantic proximity Read ↗

A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.Semantic proximity Read ↗

Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability.Semantic proximity Read ↗

Evolutionary Trajectory of the Tet(X) Family: Critical Residue Changes towards High-Level Tigecycline ResistanceSemantic proximity Read ↗

Comprehensive exploration of the translocation, stability and substrate recognition requirements in VIM-2 lactamaseSemantic proximity Read ↗

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