Evidence map›Paper›PMID 39926229›Full record

ArticleRSC advances2025

Chromogenic hydroxyanthraquinone-based enzyme substrates for the detection of microbial β-d-galactosidase, β-d-glucuronidase and β-d-ribosidase.

Michael Burton, Amy Garcha, Emma C L Marrs, John D Perry, Stephen P Stanforth, Graeme Turnbull, Hayley J Turner

Abstract read
In one paragraph

Article in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Michael BurtonGlycosynth Ltd 14 Craven Court, Winwick Quay, Cheshire Warrington WA2 8QU UK g.turnbull@northumbria.ac.uk.
Amy GarchaGlycosynth Ltd 14 Craven Court, Winwick Quay, Cheshire Warrington WA2 8QU UK g.turnbull@northumbria.ac.uk.
Emma C L MarrsDepartment of Microbiology, Freeman Hospital Newcastle upon Tyne NE7 7DN UK.
John D PerryDepartment of Microbiology, Freeman Hospital Newcastle upon Tyne NE7 7DN UK.
Stephen P StanforthDepartment of Applied Sciences, Northumbria University Newcastle upon Tyne NE1 8ST UK.ORCID https://orcid.org/0000-0003-1994-3335
Graeme TurnbullDepartment of Applied Sciences, Northumbria University Newcastle upon Tyne NE1 8ST UK.ORCID https://orcid.org/0000-0003-2606-3387
Hayley J TurnerGlycosynth Ltd 14 Craven Court, Winwick Quay, Cheshire Warrington WA2 8QU UK g.turnbull@northumbria.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Di-β-d-galactopyranoside derivatives of quinizarin (1,4-dihydroxyanthraquinone) and anthrarufin (1,5-dihydroxyanthraquinone) were evaluated as microbial enzyme substrates in Columbia agar medium for the detection of clinically important microorganisms. Furthermore, these substrates were evaluated both in the presence and absence of iron salts which could chelate to the aglycone after microbial hydrolysis of the substrate. The quinizarin-based substrate resulted in the formation of black microbial colonies in the presence of iron salts and orange colonies in their absence. In contrast, yellow-coloured microbial colonies were observed with the anthrarufin-based substrate regardless of whether iron salts were present or not. 1-Hydroxyanthraquinone-β-d-galactopyranoside also resulted in yellow-coloured microbial colonies in the absence of iron salts and an extended study of this substrate using 38 clinical strains of

Identifiers

PMID39926229
PMCPMC11804412

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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.