ArticleAntibiotics (Basel, Switzerland)2014
Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution.
Article in Antibiotics (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed.
- Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands.Chembiochem : a European journal of chemical biology · 2026Article
- Molecular Characterization and In Silico Functional Insights into Carbapenem Resistance in ClinicalPathogens (Basel, Switzerland) · 2026Article
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Development of Water-Trapping Pyrrole-2-carboxylic Acids as Broad-Spectrum Metallo-β-lactamase Inhibitors.Journal of medicinal chemistry · 2026Article
- Biochemical and structural analyses of metallo-β-lactamase VIM-28: impact of substitutions at residues 224 and 228 on substrate profile, stability, and zinc affinity.Microbiology spectrum · 2026Article
- An integrated phenotypic and genomic approach to characterize MBL-producing Enterobacterales strains circulating in a Sicilian transplant center.Microbiology spectrum · 2026Article
- Evaluation of the rapid lateral flow assay (LFA) for detection of five major carbapenemase enzyme families in genotypically characterised bacterial isolates.The Indian journal of medical research · 2025Article
- Dynamically chiral phosphonic acid-type metallo-β-lactamase inhibitors.Communications chemistry · 2025Article
- The genetic context of blaIMP varies among bacterial families from One Health sources.PloS one · 2025Article
- The impact of zinc supplementation on carbapenem MICs among bacteria expressing IMP metallo-beta-lactamase.Access microbiology · 2025Article
- Characterization of acquired β-lactamases inMicrobiology spectrum · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- The interaction of the azetidine thiazole side chain with the active site loop (ASL) 3 drives the evolution of IMP metallo-β-lactamase against tebipenem.Antimicrobial agents and chemotherapy · 2024Article
- Structural role of K224 in taniborbactam inhibition of NDM-1.Antimicrobial agents and chemotherapy · 2024Article
- In silico designing and immunoinformatics analysis of a novel peptide vaccine against metallo-beta-lactamase (VIM and IMP) variants.PloS one · 2023Article
- ROCker Models for Reliable Detection and Typing of Short-Read Sequences Carrying β-Lactamase Genes.mSystems · 2022Article
- Studies on the Reactions of Biapenem with VIM Metallo β-Lactamases and the Serine β-Lactamase KPC-2.Antibiotics (Basel, Switzerland) · 2022Article
- A multiscale approach to predict the binding mode of metallo beta-lactamase inhibitors.Proteins · 2022Article
- Article
- Dual Activity BLEG-1 fromInternational journal of molecular sciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The production of β-lactamase enzymes is one of the most distributed resistance mechanisms towards β-lactam antibiotics. Metallo-β-lactamases constitute a worrisome group of these kinds of enzymes, since they present a broad spectrum profile, being able to hydrolyze not only penicillins, but also the latest generation of cephalosporins and carbapenems, which constitute at present the last resource antibiotics. The VIM, IMP, and NDM enzymes comprise the main groups of clinically relevant metallo-β-lactamases. Here we present an update of the features of the natural variants that have emerged and of the ones that have been engineered in the laboratory, in an effort to find sequence and structural determinants of substrate preferences. This knowledge is of upmost importance in novel drug design efforts. We also discuss the advances in knowledge achieved by means of in vitro directed evolution experiments, and the potential of this approach to predict natural evolution of metallo-β-lactamases.
Indexed as
Identifiers
What OpenQuestion holds
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.