Evidence map›Paper›PMID 41195167›Full record

ArticleRSC chemical biology2026

Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2.

Cassandra R Kennedy, Katherine A McPhie, Aini Vuorinen, Jane Dudley-Fraser, Diego Esposito, Sarah Maslen, William J McCarthy, Jonathan Pettinger, J Mark Skehel, Jacob Bush and 2 more

Abstract read
In one paragraph

Article in RSC chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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.

Cassandra R KennedyMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.
Katherine A McPhieMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.ORCID https://orcid.org/0000-0001-6525-7235
Aini VuorinenProteomics Science Technology Platform, The Francis Crick Institute 1 Midland Road London NW1 1AT UK.
Jane Dudley-FraserMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.ORCID https://orcid.org/0000-0003-1571-3524
Diego EspositoMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.ORCID https://orcid.org/0000-0003-4042-8856
Sarah MaslenProteomics Science Technology Platform, The Francis Crick Institute 1 Midland Road London NW1 1AT UK.
William J McCarthyMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.ORCID https://orcid.org/0000-0002-2858-076X
Jonathan PettingerCrick-GSK Biomedical LinkLabs, GSK, Gunnels Wood Road, Stevenage Hertfordshire, SG1 2NY UK david.x.house@gsk.com.
J Mark SkehelProteomics Science Technology Platform, The Francis Crick Institute 1 Midland Road London NW1 1AT UK.
Jacob BushCrick-GSK Biomedical LinkLabs, GSK, Gunnels Wood Road, Stevenage Hertfordshire, SG1 2NY UK david.x.house@gsk.com.ORCID https://orcid.org/0000-0001-7165-0092
David HouseCrick-GSK Biomedical LinkLabs, GSK, Gunnels Wood Road, Stevenage Hertfordshire, SG1 2NY UK david.x.house@gsk.com.ORCID https://orcid.org/0000-0002-9635-2451
Katrin RittingerMolecular Structure of Cell Signalling Laboratory, The Francis Crick Institute 1 Midland Road London NW1 1AT UK katrin.rittinger@crick.ac.uk.ORCID https://orcid.org/0000-0002-7698-4435

Funding

Wellcome Trust CC1063Wellcome Trust CC2075
6 · The paper itself

Abstract

As the global fight against antimicrobial resistance in bacteria becomes increasingly pressing, new tool compounds are needed to study and evaluate novel therapeutic targets. Here, cysteine-directed fragment-based drug discovery is coupled with high throughput chemistry direct-to-biology screening to target the catalytic cysteine of a family of bacterial effector proteins, the novel E3 ligases (NELs) from

Identifiers

PMID41195167
PMCPMC12584752

What OpenQuestion holds

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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.