ArticleNature chemical biology2012
Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 55 citations in OpenAlex.
- Predatory myxobacteria lay at the cross-roads of metallo-β-lactamase evolution.Communications biology · 2026Article
- Structural insights into the activity of carbapenemases: understanding the mechanism of action of current inhibitors and informing the design of new carbapenem adjuvants.RSC medicinal chemistry · 2025Review
- Biochemical properties and substrate specificity of GOB-38 in Elizabethkingia anophelis.Scientific reports · 2025Article
- The impact of zinc supplementation on carbapenem MICs among bacteria expressing IMP metallo-beta-lactamase.Access microbiology · 2025Article
- Exploiting the fitness cost of metallo-β-lactamase expression can overcome antibiotic resistance in bacterial pathogens.Nature microbiology · 2025Article
- In-cell kinetic stability is an essential trait in metallo-β-lactamase evolution.Nature chemical biology · 2023Article
- Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface.Current opinion in chemical biology · 2022Review
- Exploring the Role of L10 Loop in New Delhi Metallo-β-lactamase (NDM-1): Kinetic and Dynamic Studies.Molecules (Basel, Switzerland) · 2021Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- Molecular Evolution of Transition Metal Bioavailability at the Host-Pathogen Interface.Trends in microbiology · 2021Review
- Visualizing the superfamily of metallo-β-lactamases through sequence similarity network neighborhood connectivity analysis.Heliyon · 2021Article
- Metallo-β-Lactamase Inhibitors Inspired on Snapshots from the Catalytic Mechanism.Biomolecules · 2020Review
- Carbapenemases: TransformingBiomolecules · 2020Review
- β-Lactamases and β-Lactamase Inhibitors in the 21st Century.Journal of molecular biology · 2019Review
- The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase.Nature communications · 2019Article
- The Reaction Mechanism of Metallo-β-Lactamases Is Tuned by the Conformation of an Active-Site Mobile Loop.Antimicrobial agents and chemotherapy · 2019Article
- Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases.The FEBS journal · 2019Article
- Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Antimicrobial agents and chemotherapy · 2018Article
- Embelin Restores Carbapenem Efficacy against NDM-1-Positive Pathogens.Frontiers in microbiology · 2018Article
- Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity.ACS infectious diseases · 2017Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent β-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations.
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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.