Evidence map›Paper›PMID 31191895›Full record

ArticleChemical science2019

A simple, robust, universal assay for real-time enzyme monitoring by signalling changes in nucleoside phosphate anion concentration using a europium(iii)-based anion receptor.

Sarah H Hewitt, Rozee Ali, Romain Mailhot, Chloe R Antonen, Charlotte A Dodson, Stephen J Butler

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Sarah H HewittDepartment of Chemistry , Loughborough University , Epinal Way , Loughborough , LE11 3TU , UK . Email: S.J.Butler@lboro.ac.uk.
Rozee AliDepartment of Chemistry , Loughborough University , Epinal Way , Loughborough , LE11 3TU , UK . Email: S.J.Butler@lboro.ac.uk.
Romain MailhotDepartment of Chemistry , Loughborough University , Epinal Way , Loughborough , LE11 3TU , UK . Email: S.J.Butler@lboro.ac.uk.
Chloe R AntonenDepartment of Chemistry , Loughborough University , Epinal Way , Loughborough , LE11 3TU , UK . Email: S.J.Butler@lboro.ac.uk.
Charlotte A DodsonDepartment of Pharmacy & Pharmacology , University of Bath , Claverton Down , Bath , BA2 7AY , UK.ORCID 0000-0002-8403-726X
Stephen J ButlerDepartment of Chemistry , Loughborough University , Epinal Way , Loughborough , LE11 3TU , UK . Email: S.J.Butler@lboro.ac.uk.ORCID 0000-0001-8109-3330
Loughborough University · GBUniversity of Bath · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Enzymes that consume and produce nucleoside polyphosphate (NPP) anions represent major targets in drug discovery. For example, protein kinases are one of the largest classes of drug targets in the fight against cancer. The accurate determination of enzyme kinetics and mechanisms is a critical aspect of drug discovery research. To increase confidence in the selection of lead drug compounds it is crucial that pharmaceutical researchers have robust, affordable assays to measure enzyme activity accurately. We present a simple, sensitive microplate assay for real-time monitoring of a range of pharmaceutically important enzyme reactions that generate NPP anions, including kinases and glycosyltransferases. Our assay utilises a single, stable europium(iii) complex that binds reversibly to NPP anions, signalling the dynamic changes in NPP product/substrate ratio during an enzyme reaction using time-resolved luminescence. This supramolecular approach to enzyme monitoring overcomes significant limitations in existing assays, obviating the need for expensive antibodies or equipment, chemically labelled substrates or products and isolation or purification steps. Our label and antibody-free method enables rapid and quantitative analysis of enzyme activities and inhibition, offering a potentially powerful tool for use in drug discovery, suitable for high-throughput screening of inhibitors and accurate measurements of enzyme kinetic parameters.

Identifiers

PMID31191895
PMCPMC6540902
OpenAlexW2943293815

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.