Evidence map›Paper›PMID 34337941›Full record

ArticleJournal of medicinal chemistry2021

High-Throughput Crystallography Reveals Boron-Containing Inhibitors of a Penicillin-Binding Protein with Di- and Tricovalent Binding Modes.

Hector Newman, Alen Krajnc, Dom Bellini, Charles J Eyermann, Grant A Boyle, Neil G Paterson, Katherine E McAuley, Robert Lesniak, Mukesh Gangar, Frank von Delft and 4 more

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

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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

14 authors.

Hector NewmanSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K.
Alen KrajncDepartment of Chemistry and the Ineos Oxford Institute of Antimicrobial Research, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, U.K.ORCID 0000-0001-7822-1944
Dom BelliniSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K.
Charles J EyermannDrug Discovery and Development Centre (H3D), University of Cape Town, Rondebosch 7701, South Africa.
Grant A BoyleDrug Discovery and Development Centre (H3D), University of Cape Town, Rondebosch 7701, South Africa.
Neil G PatersonDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0DE, U.K.
Katherine E McAuleyDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0DE, U.K.
Robert LesniakDepartment of Chemistry and the Ineos Oxford Institute of Antimicrobial Research, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, U.K.
Mukesh GangarDrug Discovery and Development Centre (H3D), University of Cape Town, Rondebosch 7701, South Africa.
Frank von DelftDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot OX11 0DE, U.K.ORCID 0000-0003-0378-0017
Jürgen BremDepartment of Chemistry and the Ineos Oxford Institute of Antimicrobial Research, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, U.K.ORCID 0000-0002-0137-3226
Kelly ChibaleDrug Discovery and Development Centre (H3D), University of Cape Town, Rondebosch 7701, South Africa.ORCID 0000-0002-1327-4727
Christopher J SchofieldDepartment of Chemistry and the Ineos Oxford Institute of Antimicrobial Research, Chemistry Research Laboratory, 12 Mansfield Road, Oxford OX1 3TA, U.K.ORCID 0000-0002-0290-6565
Christopher G DowsonSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, U.K.ORCID 0000-0002-8294-8836

Funding

Cancer Research UK 24759Medical Research Council MR/N002679/1Medical Research Council MR/P007503/1Medical Research Council MR/S014934/1Wellcome TrustWellcome Trust 106244/Z/14/Z
6 · The paper itself

Abstract

The effectiveness of β-lactam antibiotics is increasingly compromised by β-lactamases. Boron-containing inhibitors are potent serine-β-lactamase inhibitors, but the interactions of boron-based compounds with the penicillin-binding protein (PBP) β-lactam targets have not been extensively studied. We used high-throughput X-ray crystallography to explore reactions of a boron-containing fragment set with the

Indexed as

High-Throughput Screening AssaysAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesBinding SitesBoron CompoundsCrystallography, X-RayDose-Response Relationship, DrugMicrobial Sensitivity TestsModels, MolecularMolecular StructurePenicillin-Binding ProteinsPseudomonas aeruginosaStructure-Activity RelationshipAnti-Bacterial Agentsbeta-Lactamase Inhibitorsbeta-LactamasesBoron CompoundsPenicillin-Binding Proteins

Identifiers

PMID34337941
PMCPMC9282634

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.