Evidence map›Paper›PMID 40625409›Full record

ArticleRSC advances2025

Katherine Williams, Catherine E Spencer, Kate M J de Mattos-Shipley, Anjali D Shah, Trong-Tuan Dao, Jonathan A Davies, David M Heard, Zhongshu Song, Ashley J Winter, Matthew P Crump and 2 more

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

12 authors.

Katherine WilliamsSchool of Biological Sciences, Life Sciences Building, University of Bristol 24 Tyndall Avenue Bristol BS8 1TQ UK andy.bailey@bristol.ac.uk.ORCID https://orcid.org/0000-0002-1988-8818
Catherine E SpencerSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0001-8174-0913
Kate M J de Mattos-ShipleySchool of Biological Sciences, Life Sciences Building, University of Bristol 24 Tyndall Avenue Bristol BS8 1TQ UK andy.bailey@bristol.ac.uk.ORCID https://orcid.org/0000-0002-0888-490X
Anjali D ShahSchool of Biological Sciences, Life Sciences Building, University of Bristol 24 Tyndall Avenue Bristol BS8 1TQ UK andy.bailey@bristol.ac.uk.ORCID https://orcid.org/0000-0002-3677-2972
Trong-Tuan DaoSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.
Jonathan A DaviesSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0003-2845-2394
David M HeardSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0003-3005-8222
Zhongshu SongSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.
Ashley J WinterSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0003-3684-9383
Matthew P CrumpSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0002-7868-5818
Christine L WillisSchool of Chemistry, University of Bristol Cantock's Close Bristol BS8 1TS UK.ORCID https://orcid.org/0000-0002-3919-3642
Andrew M BaileySchool of Biological Sciences, Life Sciences Building, University of Bristol 24 Tyndall Avenue Bristol BS8 1TQ UK andy.bailey@bristol.ac.uk.ORCID https://orcid.org/0000-0002-7594-3703

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maleidrides are a family of polyketide-derived natural products isolated from filamentous fungi, that can exhibit significant bioactivities. These compounds are classified according to the size of their central carbocyclic ring, to which one or more maleic anhydride moieties are attached. The studies described herein provide important insights into maleidride biosynthesis, in particular the pathways to the nonadrides scytalidin and castaneiolide, and the octadride zopfiellin. We propose a supportive role for isochorismatase-like enzymes, which are commonly encoded within maleidride biosynthetic gene clusters, in facilitating α-ketoglutarate dependent dioxygenase-mediated catalysis. This is evidenced by gene deletions as well as enzyme assays, for two maleidride biosynthetic pathways: that of zopfiellin, from

Identifiers

PMID40625409
PMCPMC12231587

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.