ReviewCurrent opinion in chemical biology2022
Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface.
Review in Current opinion in chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Identification and characterization of quorum-quenching enzyme AiiF fromApplied and environmental microbiology · 2026Article
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Acid tolerance and metabolic potential of comammox and nitrite-oxidizingISME communications · 2025Article
- The impact of zinc supplementation on carbapenem MICs among bacteria expressing IMP metallo-beta-lactamase.Access microbiology · 2025Article
- Characterization of VldE (Spr1875), a Pneumococcal Two-State l,d-Endopeptidase with a Four-Zinc Cluster in the Active Site.ACS catalysis · 2024Article
- Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis.Annual review of microbiology · 2024Review
- Probing metalloenzyme dynamics in living systems: Contemporary advances in fluorescence imaging tools and applications.Current opinion in chemical biology · 2024Review
- Rational Design of Benzobisheterocycle Metallo-β-Lactamase Inhibitors: A Tricyclic Scaffold Enhances Potency against Target Enzymes.Journal of medicinal chemistry · 2024Article
- The metallo-β-lactamases strike back: emergence of taniborbactam escape variants.Antimicrobial agents and chemotherapy · 2024Review
- TerC proteins function during protein secretion to metalate exoenzymes.Nature communications · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.Research square · 2023Article
- TerC Proteins Function During Protein Secretion to Metalate Exoenzymes.bioRxiv : the preprint server for biology · 2023Article
- Auranofin Targeting the NDM-1 Beta-Lactamase: Computational Insights into the Electronic Configuration and Quasi-Tetrahedral Coordination of Gold Ions.Pharmaceutics · 2023Article
- Metals to combat antimicrobial resistance.Nature reviews. Chemistry · 2023Review
- Gating interactions steer loop conformational changes in the active site of the L1 metallo-β-lactamase.eLife · 2023Article
- Metal retention and replacement in QueD2 protect queuosine-tRNA biosynthesis in metal-starvedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Increased zinc levels facilitate phenotypic detection of ceftazidime-avibactam resistance in metallo-β-lactamase-producing Gram-negative bacteria.Frontiers in microbiology · 2022Article
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 1 institution in 1 country.
Funding
Abstract
Metallo-β-lactamases (MBLs) are zinc-dependent hydrolases that inactivate virtually all β-lactam antibiotics. The expression of MBLs by Gram-negative bacteria severely limits the therapeutic options to treat infections. MBLs bind the essential metal ions in the bacterial periplasm, and their activity is challenged upon the zinc starvation conditions elicited by the native immune response. Metal depletion compromises both the enzyme activity and stability in the periplasm, impacting on the resistance profile in vivo. Thus, novel inhibitory approaches involve the use of chelating agents or metal-based drugs that displace the native metal ion. However, newer MBL variants incorporate mutations that improve their metal binding abilities or stabilize the metal-depleted form, revealing that metal starvation is a driving force acting on MBL evolution. Future challenges require addressing the gap between in cell and in vitro studies, dissecting the mechanism for MBL metalation and determining the metal content in situ.
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.