Evidence map›Paper›PMID 34129337›Full record

ReviewChemical reviews2021

Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.

Guillermo Bahr, Lisandro J González, Alejandro J Vila

Abstract readReview
In one paragraph

Review in Chemical reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

115 citing papers in PubMed.

  1. Lanthipeptides fromMicrobiology spectrum · 2026
    Article
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  7. Review
  8. Synergistic eradication of NDM-1Materials today. Bio · 2026
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  20. The anti-inflammatory drug celecoxib is metabolized by Pseudomonas aeruginosa CYP107S1 in vitro and in vivo.Drug metabolism and disposition: the biological fate of chemicals · 2025
    Article

55 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Guillermo BahrInstituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Universidad Nacional de Rosario, Ocampo y Esmeralda S/N, 2000 Rosario, Argentina.ORCID 0000-0003-2187-4463
Lisandro J GonzálezInstituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Universidad Nacional de Rosario, Ocampo y Esmeralda S/N, 2000 Rosario, Argentina.
Alejandro J VilaInstituto de Biología Molecular y Celular de Rosario (IBR), CONICET, Universidad Nacional de Rosario, Ocampo y Esmeralda S/N, 2000 Rosario, Argentina.ORCID 0000-0002-7978-3233

Funding

A Mechanism-Based Approach to Metallo-beta-Lactamase InhibitionR01AI100560 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI BONOMO, ROBERT A., SPENCER, JAMES · 2012 to 2022
$4.4M
Howard Hughes Medical InstituteNIAID NIH HHS R01 AI100560
6 · The paper itself

Abstract

Antimicrobial resistance is one of the major problems in current practical medicine. The spread of genes coding for resistance determinants among bacteria challenges the use of approved antibiotics, narrowing the options for treatment. Resistance to carbapenems, last resort antibiotics, is a major concern. Metallo-β-lactamases (MBLs) hydrolyze carbapenems, penicillins, and cephalosporins, becoming central to this problem. These enzymes diverge with respect to serine-β-lactamases by exhibiting a different fold, active site, and catalytic features. Elucidating their catalytic mechanism has been a big challenge in the field that has limited the development of useful inhibitors. This review covers exhaustively the details of the active-site chemistries, the diversity of MBL alleles, the catalytic mechanism against different substrates, and how this information has helped developing inhibitors. We also discuss here different aspects critical to understand the success of MBLs in conferring resistance: the molecular determinants of their dissemination, their cell physiology, from the biogenesis to the processing involved in the transit to the periplasm, and the uptake of the Zn(II) ions upon metal starvation conditions, such as those encountered during an infection. In this regard, the chemical, biochemical and microbiological aspects provide an integrative view of the current knowledge of MBLs.

Indexed as

Drug Resistance, MultipleEvolution, MolecularAnimalsbeta-Lactamase Inhibitorsbeta-LactamasesHumansbeta-Lactamase Inhibitorsbeta-Lactamases

Identifiers

PMID34129337
PMCPMC9062786

What OpenQuestion holds

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Registered trials

None linked

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.