Evidence map›Paper›PMID 31541180›Full record

ArticleScientific reports2019

Mechanistic Insights into β-Lactamase-Catalysed Carbapenem Degradation Through Product Characterisation.

Christopher T Lohans, Emily I Freeman, Emma van Groesen, Catherine L Tooke, Philip Hinchliffe, James Spencer, Jürgen Brem, Christopher J Schofield

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Virulence · 2026
    Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Dynamic Gene Clusters Mediating Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Review
  17. Review
  18. Competing off-loading mechanisms of meropenem from an l,d-transpeptidase reduce antibiotic effectiveness.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. 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

8 authors at 3 institutions in 2 countries.

Christopher T LohansDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom. christopher.lohans@queensu.ca.
Emily I FreemanDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom.
Emma van GroesenDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom.
Catherine L TookeSchool of Cellular and Molecular Medicine, University of Bristol, Bristol, BS8 1TD, United Kingdom.
Philip HinchliffeSchool of Cellular and Molecular Medicine, University of Bristol, Bristol, BS8 1TD, United Kingdom.
James SpencerSchool of Cellular and Molecular Medicine, University of Bristol, Bristol, BS8 1TD, United Kingdom.
Jürgen BremDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom.ORCID http://orcid.org/0000-0002-0137-3226
Christopher J SchofieldDepartment of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom. christopher.schofield@chem.ox.ac.uk.ORCID http://orcid.org/0000-0002-0290-6565
University of Oxford · GBUniversity of Bristol · GBQueen's University · CA

Funding

Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

β-Lactamases are a major threat to the clinical use of carbapenems, which are often antibiotics of last resort. Despite this, the reaction outcomes and mechanisms by which β-lactamases degrade carbapenems are still not fully understood. The carbapenem bicyclic core consists of a β-lactam ring fused to a pyrroline ring. Following β-lactamase-mediated opening of the β-lactam, the pyrroline may interconvert between an enamine (2-pyrroline) form and two epimeric imine (1-pyrroline) forms; previous crystallographic and spectroscopic studies have reported all three of these forms in the contexts of hydrolysis by different β-lactamases. As we show by NMR spectroscopy, the serine β-lactamases (KPC-2, SFC-1, CMY-10, OXA-23, and OXA-48) and metallo-β-lactamases (NDM-1, VIM-1, BcII, CphA, and L1) tested all degrade carbapenems to preferentially give the Δ

Identifiers

PMID31541180
PMCPMC6754457
OpenAlexW2974597179

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.