Evidence map›Paper›PMID 41308195›Full record

ArticleJournal of the American Chemical Society2025

Light-Activated Metal-Dependent Protein Degradation: A Heterobifunctional Ruthenium(II) Photosensitizer Targeting New Delhi Metallo-β-lactamase 1.

Lars Stevens-Cullinane, Thomas W Rees, Calum Evans, Po-Yu Ho, Mika Kintzel, Yew Mun Yip, Ruoning Jia, Jonathan Bailey, Eleanor Clifford, Ruqaiya Alam and 13 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 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

23 authors.

Lars Stevens-CullinaneDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Thomas W ReesThe Biological Inorganic Chemistry Laboratory, The Francis Crick Institute, London, NW1 1AT, U.K.ORCID 0000-0001-7501-3461
Calum EvansDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Po-Yu HoDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Mika KintzelDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Yew Mun YipChemical Biology Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Ruoning JiaDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Jonathan BaileyThe Biological Inorganic Chemistry Laboratory, The Francis Crick Institute, London, NW1 1AT, U.K.ORCID 0000-0003-4088-8094
Eleanor CliffordDepartment of Chemistry, Imperial College London, London, W12 0BZ, U.K.
Ruqaiya AlamDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.ORCID 0009-0002-5066-9231
Sarah MaslenProteomics Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Stephane MouilleronStructural Biology Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Adrien PasquierHigh Throughput Screening Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Ok-Ryul SongHigh Throughput Screening Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Scott WarchalHigh Throughput Screening Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Joanna RedmondChemical Biology Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.ORCID 0000-0002-3200-4087
Michael HowellHigh Throughput Screening Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.ORCID 0000-0003-0912-0079
Svend KjærStructural Biology Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Mark SkehelProteomics Science and Technology Platform, The Francis Crick Institute, London, NW1 1AT, U.K.
Manuel M MüllerDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.
Eachan O JohnsonSystems Chemical Biology of Infection and Resistance Laboratory, The Francis Crick Institute, London, NW1 1AT, U.K.
Maxie M RoesslerDepartment of Chemistry, Department of Chemistry and Centre for Pulse EPR Spectroscopy (PEPR), Imperial College London, London, W12 0BZ, U.K.ORCID 0000-0002-5291-4328
Jeannine HessDepartment of Chemistry, King's College London, London, SE1 1DB, U.K.ORCID 0000-0001-5916-0728

Funding

Wellcome Trust CC2169Wellcome Trust CC2215
6 · The paper itself

Abstract

Antimicrobial resistance (AMR) is a global health threat, yet, despite this, antibiotic drug discovery has stagnated. Most compounds entering the clinic represent already discovered classes, to which bacteria already display resistance. We urgently need novel therapeutics to address this. Targeted protein degradation, typified by proteolysis-targeting chimeras (PROTACs), is a promising approach that has already seen success in oncology. A significant hurdle faced by these methods, however, is the complexity inherent in recruiting the host cell's proteolytic processes. We herein describe an approach where proteolysis is performed by a light-activated ruthenium complex, termed LAMP-D (

Indexed as

Anti-Bacterial Agentsbeta-LactamasesCoordination ComplexesLightPhotosensitizing AgentsProteolysisRutheniumEscherichia coliHumansAnti-Bacterial Agentsbeta-lactamase NDM-1beta-LactamasesCoordination ComplexesPhotosensitizing AgentsRuthenium

Identifiers

PMID41308195
PMCPMC12703741

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.