Evidence map›Paper›PMID 37408556›Full record

ReviewFrontiers in chemistry2023

Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup-emerging targets to combat antibiotic resistance.

Stefan Krco, Samuel J Davis, Pallav Joshi, Liam A Wilson, Marcelo Monteiro Pedroso, Andrew Douw, Christopher J Schofield, Philip Hugenholtz, Gerhard Schenk, Marc T Morris

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Frontiers in chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. LysR-type transcriptional regulatorFrontiers in cellular and infection microbiology · 2025
    Article
  6. Novel Metallo-β-LactamasePathogens (Basel, Switzerland) · 2023
    Article
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

10 authors.

Stefan KrcoSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Samuel J DavisSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Pallav JoshiSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Liam A WilsonChemistry Research Laboratory, Department of Chemistry, The Ineos Oxford Institute for Antimicrobial Research, Oxford University, Oxford, United Kingdom.
Marcelo Monteiro PedrosoSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Andrew DouwSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Christopher J SchofieldChemistry Research Laboratory, Department of Chemistry, The Ineos Oxford Institute for Antimicrobial Research, Oxford University, Oxford, United Kingdom.
Philip HugenholtzSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Gerhard SchenkSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Marc T MorrisSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Lactams are the most widely employed antibiotics in clinical settings due to their broad efficacy and low toxicity. However, since their first use in the 1940s, resistance to β-lactams has proliferated to the point where multi-drug resistant organisms are now one of the greatest threats to global human health. Many bacteria use β-lactamases to inactivate this class of antibiotics via hydrolysis. Although nucleophilic serine-β-lactamases have long been clinically important, most broad-spectrum β-lactamases employ one or two metal ions (likely Zn

Indexed as

antibiotic resistanceclassificationdrug developmentevolutionfunctionMetallo-β-Lactamase superfamilystructureβ-Lactamase

Identifiers

PMID37408556
PMCPMC10318434

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.