ArticleThe Journal of biological chemistry2018
Synergistic effects of functionally distinct substitutions in β-lactamase variants shed light on the evolution of bacterial drug resistance.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- Cefdinir binding to a class A β-lactamase revealed by serial cryo-crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- The Influence of Seasonality and Antimicrobial Resistance Genes on Biofilm Formation in Hospital-Acquired Resistant Bacteria.Journal of epidemiology and global health · 2026Article
- High prevalence of extended spectrum β-Lactamase producing Enterobacterales isolated from major hospitals in Gaza strip.BMC microbiology · 2026Article
- Pathogenicity ofFrontiers in cellular and infection microbiology · 2026Article
- Structural comparison of substrate-binding pockets of serine β-lactamases in classes A, C, and D.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Biofilm Formation by Hospital-Acquired Resistant Bacteria Isolated from Respiratory Samples.Journal of epidemiology and global health · 2024Article
- Restricted Rotational Flexibility of the C5α-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the GES-5 Carbapenemase.ACS infectious diseases · 2024Article
- Toward physics-based precision medicine: Exploiting protein dynamics to design new therapeutics and interpret variants.Protein science : a publication of the Protein Society · 2024Review
- Mapping the determinants of catalysis and substrate specificity of the antibiotic resistance enzyme CTX-M β-lactamase.Communications biology · 2023Article
- Phenotypic Characterization and Antibiograms of Extended-Spectrum Beta-Lactamase-ProducingInfection and drug resistance · 2023Article
- An active site loop toggles between conformations to control antibiotic hydrolysis and inhibition potency for CTX-M β-lactamase drug-resistance enzymes.Nature communications · 2022Article
- Slow Protein Dynamics Elicits New Enzymatic Functions by Means of Epistatic Interactions.Molecular biology and evolution · 2022Article
- Amplification of the ChromosomalMicrobiology spectrum · 2022Article
- Epistasis shapes the fitness landscape of an allosteric specificity switch.Nature communications · 2021Article
- Pervasive cooperative mutational effects on multiple catalytic enzyme traits emerge via long-range conformational dynamics.Nature communications · 2021Article
- Comprehensive study of antimicrobial susceptibility pattern and extended spectrum beta-lactamase (ESBL) prevalence in bacteria isolated from urine samples.Scientific reports · 2021Article
- A drug-resistant β-lactamase variant changes the conformation of its active-site proton shuttle to alter substrate specificity and inhibitor potency.The Journal of biological chemistry · 2020Article
- Molecular Mechanisms, Epidemiology, and Clinical Importance of β-Lactam Resistance inInternational journal of molecular sciences · 2020Review
- Antagonism between substitutions in β-lactamase explains a path not taken in the evolution of bacterial drug resistance.The Journal of biological chemistry · 2020Article
- Natural variants modify Klebsiella pneumoniae carbapenemase (KPC) acyl-enzyme conformational dynamics to extend antibiotic resistance.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The CTX-M β-lactamases have emerged as the most widespread extended-spectrum β-lactamases (ESBLs) in Gram-negative bacteria. These enzymes rapidly hydrolyze cefotaxime, but not the related cephalosporin, ceftazidime. ESBL variants have evolved, however, that provide enhanced ceftazidime resistance. We show here that a natural variant at a nonactive site,
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.