ReviewCurrent drug targets2016
B1-Metallo-β-Lactamases: Where Do We Stand?
Review in Current drug targets, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 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
107 citing papers in PubMed, 203 citations in OpenAlex.
- Pharmacokinetics and safety of aztreonam/avibactam for the treatment of complicated intra-abdominal infections in hospitalized adults: results from the REJUVENATE study.The Journal of antimicrobial chemotherapy · 2020Trial
- The global epidemiology and treatment of metallo-β-lactamase-producing gram-negative pathogens.JAC-antimicrobial resistance · 2026Review
- Chelate-conjugated β-lactams resensitize metallo-β-lactamase IMP-1-producing gram-negative bacteria against carbapenem antibiotics.Microbiology spectrum · 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
- Unusual case ofFrontiers in cellular and infection microbiology · 2026Review
- Genomic characterization of carbapenem-resistantFrontiers in cellular and infection microbiology · 2026Article
- Article
- Metallo Beta Lactamase Enzymes.Indian journal of microbiology · 2025Review
- Performance of disc diffusion and four commercially available MIC tests to determine mecillinam susceptibility on carbapenemase-producing Enterobacterales.Journal of clinical microbiology · 2025Article
- The Detection of Extensively Drug-ResistantMicroorganisms · 2025Article
- Exploiting the fitness cost of metallo-β-lactamase expression can overcome antibiotic resistance in bacterial pathogens.Nature microbiology · 2025Article
- Navigating the Current Treatment Landscape of Metallo-β-Lactamase-Producing Gram-Negative Infections: What are the Limitations?Infectious diseases and therapy · 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
- Probing metalloenzyme dynamics in living systems: Contemporary advances in fluorescence imaging tools and applications.Current opinion in chemical biology · 2024Review
- Design, synthesis and antibacterial activity evaluation of ebselen derivatives in NDM-1 producing bacteria.RSC medicinal chemistry · 2024Article
- Relative inhibitory activities of the broad-spectrum β-lactamase inhibitor xeruborbactam in comparison with taniborbactam against metallo-β-lactamases produced inAntimicrobial agents and chemotherapy · 2024Article
- Machine Learning Models Identify Inhibitors of New Delhi Metallo-β-lactamase.Journal of chemical information and modeling · 2024Article
- Regional dissemination of NDM-1 producingEuro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin · 2024Article
- Structural role of K224 in taniborbactam inhibition of NDM-1.Antimicrobial agents and chemotherapy · 2024Article
- Relative inhibitory activities of the broad-spectrum β-lactamase inhibitor taniborbactam against metallo-β-lactamases.Antimicrobial agents and chemotherapy · 2024Article
47 more citing papers are in PubMed but not listed here.
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 at 2 institutions in 1 country.
Funding
Abstract
Metallo-β-Lactamases (MBLs) are class Bβ-lactamases that hydrolyze almost all clinically-availableβ-lactam antibiotics. MBLs feature the distinctive αβ/βα sandwich fold of the metallo-hydrolase/oxidoreductase superfamily and possess a shallow active-site groove containing one or two divalent zinc ions, flanked by flexible loops. According to sequence identity and zinc ion dependence, MBLs are classified into three subclasses (B1, B2 and B3), of which the B1 subclass enzymes have emerged as the most clinically significant. Differences among the active site architectures, the nature of zinc ligands, and the catalytic mechanisms have limited the development of a common inhibitor. In this review, we will describe the molecular epidemiology and structural studies of the most prominent representatives of class B1 MBLs (NDM-1, IMP-1 and VIM-2) and describe the implications for inhibitor design to counter this growing clinical threat.
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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.