ReviewAnnals of the New York Academy of Sciences2013
Metallo-β-lactamase structure and function.
Review in Annals of the New York Academy of Sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 251 papers, 2 of them syntheses that pooled it.
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
251 citing papers in PubMed, 2 syntheses or guidelines pooled it, 494 citations in OpenAlex.
- Global Epidemiology and Antimicrobial Resistance of Metallo-β-Lactamase (MBL)-Producing Acinetobacter Clinical Isolates: A Systematic Review.Pathogens (Basel, Switzerland) · 2025Pooled it
- Tackling the Antibiotic Resistance Caused by Class AInternational journal of molecular sciences · 2018Pooled it
- Identification and characterization of quorum-quenching enzyme AiiF fromApplied and environmental microbiology · 2026Article
- Aztreonam-avibactam at the frontline: A dual-agent approach to metallo-β-lactamase resistance.The Journal of antibiotics · 2026Review
- From environmental reservoirs to clinical threats: the expanding resistome and genetic plasticity of Citrobacter spp.Infection · 2026Review
- Targeting the outer membrane porin OprF restores carbapenem efficacy during experimental sepsis caused by NDM-1-producing Pseudomonas aeruginosa.Scientific reports · 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
- Structure and function of persulfide dioxygenase fromiScience · 2026Article
- Application value of Xpert Carba-R combined with LAMP in the diagnosis and prognosis of carbapenem-resistant Gram-negative bacilli pneumonia.Microbiology spectrum · 2026Article
- Zinc starvation uncovers bacterial host-specific proteases that shape NDM adaptability inmBio · 2026Article
- High-pathogenicity island enhances NDM-5 activity and drives global spread of Escherichia coli ST410.The ISME journal · 2026Article
- The Role of Zinc Against Bacterial Infections in Neonates, Children, and Adults: A Scoping Review from the Available Evidence of Randomized Controlled Trials About Zinc Supplementation to New Research Opportunities.Antibiotics (Basel, Switzerland) · 2026Review
- Activity of aztreonam-avibactam, cefiderocol, and cefepime-taniborbactam against a global collection of genetically characterized metallo-β-lactamase-producing Enterobacterales.Antimicrobial agents and chemotherapy · 2026Article
- Cost-Effectiveness Analysis of Aztreonam-Avibactam (ATM-AVI) Versus Colistin + Meropenem (COL + MER) for the Treatment of Infections Caused by Metallo-β-Lactamase (MBL)-Producing Enterobacterales in Italy.PharmacoEconomics · 2025Article
- Unraveling the genetic architecture of anti-nutritional factors in soybean (Glycine max.) for nutritional enhancement.Scientific reports · 2025Article
- Whole-genome sequencing reveals resistance mechanisms and molecular epidemiology of carbapenem-resistant Pseudomonas aeruginosa bloodstream infections.BMC microbiology · 2025Article
- Clinical carbapenem-resistantMicrobiology spectrum · 2025Article
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.Nucleic acids research · 2025Article
- Cefiderocol "under siege"? Understanding the rise of NDM-mediated resistance to novel agents.Chemical science · 2025Article
- Suppression of gut colonization by multidrug-resistant Escherichia coli clinical isolates through cooperative niche exclusion.Nature communications · 2025Article
191 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
1 author at 1 institution in 1 country.
Funding
Abstract
β-Lactam antibiotics are the most commonly used antibacterial agents and growing resistance to these drugs is a concern. Metallo-β-lactamases are a diverse set of enzymes that catalyze the hydrolysis of a broad range of β-lactam drugs including carbapenems. This diversity is reflected in the observation that the enzyme mechanisms differ based on whether one or two zincs are bound in the active site that, in turn, is dependent on the subclass of β-lactamase. The dissemination of the genes encoding these enzymes among Gram-negative bacteria has made them an important cause of resistance. In addition, there are currently no clinically available inhibitors to block metallo-β-lactamase action. This review summarizes the numerous studies that have yielded insights into the structure, function, and mechanism of action of these enzymes.
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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.