Evidence map›Paper›PMID 33910990›Full record

ArticlemSphere2021

Cryptic β-Lactamase Evolution Is Driven by Low β-Lactam Concentrations.

Christopher Fröhlich, João A Gama, Klaus Harms, Viivi H A Hirvonen, Bjarte A Lund, Marc W van der Kamp, Pål J Johnsen, Ørjan Samuelsen, Hanna-Kirsti S Leiros

Open access · goldAbstract read
In one paragraph

Article in mSphere, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Evolutionary rewiring of the dynamic network underpinning allosteric epistasis in NS1 of the influenza A virus.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Evolution of β-lactamase-mediated cefiderocol resistance.The Journal of antimicrobial chemotherapy · 2022
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436.Acta crystallographica. Section F, Structural biology communications · 2021
    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

9 authors at 3 institutions in 2 countries.

Christopher FröhlichThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT The Arctic University of Norway, Tromsø, Norway christofrohlich@gmail.com hanna-kirsti.leiros@uit.no.ORCID 0000-0003-2682-2267
João A GamaDepartment of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0003-0967-6616
Klaus HarmsDepartment of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0003-1454-0692
Viivi H A HirvonenSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-5682-2738
Bjarte A LundHylleraas Centre for Quantum Molecular Sciences, Department of Chemistry, UiT The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0001-9141-0555
Marc W van der KampSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-8060-3359
Pål J JohnsenDepartment of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0002-6455-6433
Ørjan Samuelsen *Department of Pharmacy, UiT The Arctic University of Norway, Tromsø, Norway.ORCID 0000-0002-5525-2614
Hanna-Kirsti S LeirosThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT The Arctic University of Norway, Tromsø, Norway christofrohlich@gmail.com hanna-kirsti.leiros@uit.no.ORCID 0000-0002-2726-6322
UiT The Arctic University of Norway · NOUniversity of Bristol · GBUniversity Hospital of North Norway · NO

Funding

Biotechnology and Biological Sciences Research Council BB/M026280/1Medical Research Council MR/N0137941/1
6 · The paper itself

Abstract

Our current understanding of how low antibiotic concentrations shape the evolution of contemporary β-lactamases is limited. Using the widespread carbapenemase OXA-48, we tested the long-standing hypothesis that selective compartments with low antibiotic concentrations cause standing genetic diversity that could act as a gateway to developing clinical resistance. Here, we subjected

Indexed as

Evolution, MolecularAnti-Bacterial Agentsbeta-Lactamasesbeta-LactamsEscherichia coliEscherichia coli ProteinsGenetic VariationMicrobial Sensitivity TestsPlasmidsAnti-Bacterial Agentsbeta-lactamase OXA-48, E colibeta-Lactamasesbeta-LactamsEscherichia coli Proteinscarbapenemcarbapenemasecatalytic efficiencyceftazidimecryptic evolutionEscherichia coliOXA-48resistance developmentstructural flexibilitysub-MIC

Identifiers

PMID33910990
PMCPMC8092134
OpenAlexW3158020980

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.