Evidence map›Paper›PMID 32545682›Full record

ArticleBiomolecules2020

Bicyclic Boronates as Potent Inhibitors of AmpC, the Class C β-Lactamase from

Pauline A Lang, Anete Parkova, Thomas M Leissing, Karina Calvopiña, Ricky Cain, Alen Krajnc, Tharindi D Panduwawala, Jules Philippe, Colin W G Fishwick, Peteris Trapencieris and 3 more

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. In vitro activity and resistance mechanisms of novel antimicrobial agents against metallo-β-lactamase producers.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
  7. Review
  8. Identification of Potential Inhibitors of Three NDM Variants ofCurrent computer-aided drug design · 2025
    Article
  9. Review
  10. Article
  11. Class C β-Lactamases: Molecular Characteristics.Clinical microbiology reviews · 2022
    Review
  12. Review
  13. Studies on enmetazobactam clarify mechanisms of widely used β-lactamase inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

13 authors at 4 institutions in 3 countries.

Pauline A LangDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0003-3187-1469
Anete ParkovaLatvian Institute of Organic Synthesis, LV-1006 Riga, Latvia.
Thomas M LeissingDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.
Karina CalvopiñaDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0003-0780-4645
Ricky CainSchool of Chemistry, University of Leeds, Leeds LS2 9JT, UK.
Alen KrajncDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0001-7822-1944
Tharindi D PanduwawalaDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0001-7095-1336
Jules PhilippeJacobs University Bremen gGmbH, 28759 Bremen, Germany.
Colin W G FishwickSchool of Chemistry, University of Leeds, Leeds LS2 9JT, UK.
Peteris TrapencierisLatvian Institute of Organic Synthesis, LV-1006 Riga, Latvia.
Malcolm G P PageJacobs University Bremen gGmbH, 28759 Bremen, Germany.ORCID 0000-0002-0276-8174
Christopher J SchofieldDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0002-0290-6565
Jürgen BremDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Oxford OX1 3TA, UK.ORCID 0000-0002-0137-3226
University of Oxford · GBConstructor University · DELatvijas Organiskās Sintēzes Institūts · LVUniversity of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S50676X/1MRF MRF-145-0004-TPG-AVISOMRF_ MRF-145-0004-TPG-AVISO
6 · The paper itself

Abstract

Resistance to β-lactam antibacterials, importantly via production of β-lactamases, threatens their widespread use. Bicyclic boronates show promise as clinically useful, dual-action inhibitors of both serine- (SBL) and metallo- (MBL) β-lactamases. In combination with cefepime, the bicyclic boronate taniborbactam is in phase 3 clinical trials for treatment of complicated urinary tract infections. We report kinetic and crystallographic studies on the inhibition of AmpC, the class C β‑lactamase from

Indexed as

Anti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic AcidsCrystallography, X-RayCyclizationDrug Resistance, BacterialEscherichia coliMicrobial Sensitivity TestsAmpC beta-lactamasesAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic Acidsantibiotic resistancebicyclic boronate inhibitorsmetallo- and serine-β-lactamase inhibitiontransition state analogue.vaborbactamVNRX-5133/taniborbactamβ-lactam antibacterial

Identifiers

PMID32545682
PMCPMC7356297
OpenAlexW3034560589

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.